Mineral Pictures Index

Mineral Pictures Index If youre interested in rock collecting, you know that rocks you find in the real world rarely look like the polished specimens you see you rock shops or museums. In this index, youll find pictures of minerals like those youll most likely encounter in your expeditions. This list starts with the handful of common minerals called the rock-forming minerals, followed by the most common accessory minerals- youll find them scattered in many different rocks but seldom in large amounts. Next, youll see a set of rare or notable minerals, some of which are common in commercial rock shops. Finally, you can check out some special galleries designed to help you to identify your specimens. Rock-Forming Minerals Rock-forming minerals are among the most common (and least valuable) minerals in the world. They form the basis of igneous, metamorphic, and sedimentary rocks, and are used to classify and name rocks. Some examples include: Biotite- Black mica, common in igneous rocks. Calcite- The most common carbonate mineral, making up limestone. Dolomite- Magnesium-rich cousin to calcite. Feldspar- A group making up the most common mineral in the crust. (Feldspar Gallery) Hornblende- The most common mineral of the amphibole group. Muscovite- White mica, found in all kinds of rocks. Olivine- A green mineral found strictly in igneous rocks. Pyroxene- A group of dark minerals of igneous and metamorphic rocks. Quartz- Familiar as crystals and as noncrystalline chalcedony. (Quartz/Silica Gallery) Accessory Minerals   Accessory minerals may be included in any rock you pick up, but unlike rock-forming minerals, they are not a basic part of the rock. In other words, a rock must contain quartz, feldspar, and mica  in order to be classified as granite. If the rock also happens to contain the mineral titanite, the rock is still granite and the titanite is classified as an accessory mineral.  Accessory minerals are also not  particularly abundant, and so they may be more valuable than rock-forming minerals. Some examples include: Andalusite- Makes collectible crossed crystals. Anhydrite- What gypsum becomes deep underground. Apatite- The phosphate mineral making up teeth and bones. Aragonite- Calcites close carbonate cousin. Barite- A heavy sulfate sometimes found in roses. Bornite- Peacock ore copper mineral tarnishes a crazy blue-green. Cassiterite- Ancient and principal ore of tin. Chalcopyrite- Foremost ore of copper. Chlorite- The green mineral of many metamorphic rocks. Corundum- Natural alumina, sometimes known as sapphire and ruby. Epidote- Metamorphic mineral of a pistachio/avocado green color. Fluorite- Every rockhound has a piece of this soft, colorful mineral. Galena- A heavy, glittering mineral, principal ore of lead metal. Garnet Almandine- The true garnet-red garnet mineral. Andradite- Green crystals from central California. Grossular- A greenish garnet illustrated by a well-formed crystal. Pyrope- Wine-colored grains in a California eclogite. Spessartine- A honey-colored set of crystals from China. Uvarovite- Emerald-green crystals from Russia. Goethite- The brown oxide mineral of soils and iron ore. Graphite- The stuff of pencils has more rugged uses too. Gypsum- Shown in its prettiest form, desert roses. Halite- Also known as rock salt, this evaporite mineral sits at your table. Hematite- Iron oxide mineral of many forms including this kidney ore. Ilmenite- Black titanium ore lurks in heavy sands. Kyanite- A sky-blue mineral formed by high-pressure metamorphism. Lepidolite- Lithium mica mineral with a fine lilac color. Leucite- Feldspathoid mineral also called white garnet. Magnetite- Magnetic iron oxide also known as lodestone. Marcasite- Close crystal cousin of pyrite. Nepheline- Feldspathoid mineral well known to potters. Phlogopite- Brown mica mineral closely related to biotite. Prehnite- Bottle-green mineral of low-grade metamorphic rocks. Psilomelane- Manganese oxides make up this black crusty mineral. Pyrite- Fools gold and the most important sulfide mineral. Pyrolusite- The black manganese mineral of dendrites. Rutile- Needles of this oxide mineral occur in many rocks. Serpentine- The group of green minerals that yields asbestos. Sillimanite- Indicator mineral for high grades of metamorphism. Sphalerite- The major zinc ore and an interesting mineral. Spinel- Rugged oxide mineral of metamorphosed limestones. Staurolite- A typical crossed pair of crystals in a mica schist matrix. Talc- The softest mineral of them all. Tourmaline- The common black variety called schorl. Zeolites- Group of low-temperature minerals with many industrial uses. Zircon- Both a gemstone and a precious source of geologic information. Uncommon Minerals and Varieties This collection of minerals includes metals, ores, and gems. Some of these gold, diamond, and beryl for example are among the most valuable and coveted minerals in the world. If you find these in your rock hunting excursions, be sure to keep them safe. Some examples include: Amethyst- The purple form of crystalline quartz. Axinite- Minor silicate of striking crystal form and color. Benitoite- Very blue, very rare and weird ring silicate mineral. Beryl- Gemstone of many names, including emerald. Borax- This household commonplace is mined in desert lakebeds. Celestine- Pale, sky-blue strontium carbonate. Cerussite- Spiky gray lead carbonate. Chrysocolla- Bright green-blue mineral found near copper ore. Cinnabar- Lipstick-red mineral and major ore of mercury. Copper- Native metal shown in its natural wiry form. Cuprite- Red copper ore and sometimes spectacular specimen stone. Diamond- Natural diamond crystal from the Congo. Dioptase- Bright-green crystalline sign of copper deposits. Dumortierite- Blue boron mineral of gneisses and schists. Eudialyte- Striking red vein-maker in nepheline syenites. Fuchsite- Chromium colors this mica mineral a flashy green. Gold- The native metal shown in an Alaskan nugget. Hemimorphite- Handsome pale crusts of hydrous zinc silicate. Herkimer Diamond Quartz- Doubly terminated crystals from New York. Labradorite- The butterfly of the feldspars has dazzling blue schiller. Lazurite- Ancient mineral source of ultramarine pigment. Magnesite- Magnesium carbonate ore mineral. Malachite- Ultra-green copper carbonate, a favorite mineral of carvers. Molybdenite- Soft metallic mineral and ore of molybdenum. Opal- Precious silica mineraloid may display a rainbow of colors. Platinum- Rare crystalline nuggets of the native metal. Pyromorphite- Flashy green lead phosphate mineral. Pyrophyllite- Soft mineral closely resembling talc. Rhodochrosite- Calcites manganese cousin with distinctive rosy color. Ruby- Deep-red gemmy variety of corundum. Scapolite- Streaked clear crystals of metamorphosed limestones. Siderite- Brown iron carbonate mineral. Silver- Wiry specimen of the rare native metal. Smithsonite- Carbonate of zinc appears in many forms. Sodalite- Deep blue feldspathoid and a rock carvers staple. Sulfur- Delicate crystals accumulate around a volcanic vent. Sylvite- Red potassium mineral distinguished by its bitter taste. Titanite- Collectible brown crystalline mineral once known as sphene. Topaz- Hardness and good crystals make it a popular mineral. Turquoise- The most precious phosphate mineral. Ulexite- One of many borate minerals, ulexite forms the unique TV rock. Variscite- This phosphate comes in veins like slabs of green candy. Willemite- Prized by collectors for its bright fluorescence. Witherite- Scarce barium carbonate mineral. Tools for Identifying Minerals It isnt always easy to identify minerals, even if theyre fairly common. Fortunately, there are tools used by geologists to aid in identification. Special tests for luster and streak can help; so too can these galleries of relatively common minerals of different colors. Black Minerals Blue and Purple Minerals Brown Minerals Green Minerals Red and Pink Minerals Yellow Minerals Mineral Habits Mineral Lusters Mineral Streak Mineraloids

How to Calculate PSAT Score 3-Step Score Calculator

How to Calculate PSAT Score 3-Step Score Calculator SAT / ACT Prep Online Guides and Tips If you’re struggling to calculate your PSAT score, then it sounds like you’re in need of a handy PSAT score calculator! In this guide, we offeryou step-by-step instructions on how to calculate PSAT scores. To begin, we'll look at how the PSAT is scored and what â€Å"equating† means. We'll then go overhow to calculate various PSAT scores before finishing with an explanation on how a PSAT score calculatorcan help you get the PSAT score you want. How Is the PSAT Scored? The PSAT is scored on a scale of 320-1520 in 10-point increments. Your total PSAT scoreis the sum of your Math and Evidence-Based Reading and Writing (EBRW) section scores. (EBRW is a combination of your Reading and Writing and Language scores). These two sections areeach scored on ascale of 160-760, which is equivalent to half the total score range. But there aren't 1,520 questions on the PSAT, sowhere do these numbers come from? In reality,your Math and EBRW scores start outas raw scores. A raw score is simply the number of questions you answered correctly. So if I were to get 40 Reading questions right, my raw Reading score would be 40. (Note that the PSAT uses rights-only scoring, so you'll never lose any points for incorrect answers.) Next, your raw scores for Math, Reading, and Writing and Language (we'll refer to this section as"Writing" from now on) are converted into finalscaled scores using a special equating process. The College Board (the creators of the PSAT) uses equating toaccount for slight differences in difficulty among tests, making it so thatascaled PSAT score always indicates the same level of ability, regardless of test. Here’s how the College Boarddescribes the equating process used for the PSAT: â€Å"This conversion process adjusts for slight differences in difficulty among versions of the test and provides a score that is equated, or consistent, across forms. This process ensures that no student receives an advantage or disadvantage from taking a particular form of the test on a particular day;* a score of 400 on one test form is equivalent to a score of 400 on another test form.† *Emphasis mine. Ultimately, what this means isthat raw scores will not alwaysconvert into the same scaled scores on different PSATs. Here's an example to illustrate this concept:on this practice PSAT, you can see that a 23 raw Math score converts into 540, but on this practice PSAT,23 converts into 510 instead. So are raw scores and scaled scores the only scores you'll get on the PSAT? Not at all!In addition, you’ll receivesubscores and cross-test scores (the same as those on the SAT) as well as aNational Merit Selection Index score. Subscores measure specific skills in each section on ascale of 1-15, whilecross-test scoresmeasureyour understanding ofhistory/social studies and science questions on a scale of8-38. The Selection Indexis perhaps one of the most unique scores you'll get; it has a score range of 48-228 and is used to determine your eligibility for the National Merit Scholarship Program. To qualify for the program, you must earn a Selection Index score at or above your state’scutoff score. Now, let'scalculate PSAT score areas together! Are raw PSAT scores as tasty as raw cookie dough? How to Calculate PSAT Score: Raw Scaled Here, we'llshow you how to calculate yourraw and scaled (section) PSAT scores. If you'd like to calculateyour own scores as you read along, make sure you have access to the answer key for whichever official PSAT practice testyou took. This will act as your PSAT score calculator. Note that all of the example charts and conversions below are based onthescoring guidetoPSAT Practice Test #1. Step 1: Determine Raw Scores Raw scores are a relatively easy-to-calculate PSAT score area. Remember,raw scores equal the number of correct answers you got.In other words,the highest raw score you can earn on a section will be the same as the total number of questions in that section. Each of the three PSAT sections - Reading, Writing, and Math - contains a different total number of questions, or a different raw score range. Math is the only section that's actually divided into two subsections, No Calculator and Calculator, each of which has its own raw score range. Here is an overview of the raw score ranges on the PSAT: PSAT Section Reading Writing and Language Math No Calculator Calculator Raw Score Range 0-47 0-44 0-17 0-31 Raw Reading Score Your raw Reading score will be out of 47 points. Using your practice test’s answer key, add up all of the correct answers you earned on the Reading section to get your raw Reading score. For example, if I were to miss 13 questions on the Reading section, my raw Reading score would be 34: Raw Writing and Language Score Your raw Writing score will be out of 44 points. The Writing answer key is located next to the Readinganswer key. Once again, add up all of your correct answers on your test's answer key to getyour raw Writing score. Here's an example: Raw Math Score As I mentioned above, Math is divided into two subsections: No Calculator and Calculator. This means you’ll receive two raw Math scores that'llbe subsequentlycombined to give you a total raw Math score. The maximum number of points you can earn is17 on Math No Calculator and 31 on Math Calculator. Altogether, then, you can earn up to 48 points on Math. To calculate your raw Math score, tally your correct answers on the No Calculator and Calculator subsections. Soif I were to miss 5 points on No Calculator and 8 on Calculator, my raw Math scores would be 12 and 23, respectively: Then, combine these two scores to get your total raw Math score: Step 2: Convert to Scaled Scores Scaled, or equated, scores are the final section scores you'll receive on the PSAT. These scores use a scale of 160-760, with each accounting for half your total PSAT score. As we discussedpreviously, raw-score-to-scaled-score conversions vary slightly with each PSATdue to differences in equating formulas. Thus, theconversion charts we use for our examples below will not apply exactly to all PSATs. (Remember, our examples are all based on a specific test - PSAT Practice Test #1!) Now, let's take a look at how to calculate your scaled PSAT scores. Math Section Score Start by calculatingyour total raw Math score using the steps above. Thisscore will be out of48 points. Next, look for the "Raw Score" and "Math Section Score" columns on your practice test’s raw score conversion table. (As a reminder, conversion tables varyslightly with eachtest, so one raw Math score on one test may not convert into the same scaled Math score on another test.) On the chart, your raw Math score will directly convert into a Math section score (i.e., a scaled score). To convert your score, simply match your raw score with the corresponding Math section score. In my example above, mytotal raw Math score was 35, whichconverts into 650: Raw Score Math Section Score Raw Score Math Section Score 0 160 25 560 1 190 26 570 2 210 27 580 3 240 28 580 4 270 29 590 5 290 30 600 6 320 31 610 7 340 32 620 8 360 33 630 9 370 34 640 10 390 35 650 400 36 670 12 420 37 680 13 430 38 690 14 440 39 710 15 460 40 720 16 470 41 730 17 480 42 730 18 490 43 740 19 500 44 740 20 510 45 750 21 520 46 750 22 530 47 760 23 540 48 760 24 550 EBRW Section Score Calculating your EBRW section score requires a couple of extra steps. Like the process you followedfor figuring outyour Math section score, beginby calculating your raw Reading and Writing scores (using the steps above). These scores will be out of 47 and 44 points, respectively. Next, look for your scaled Reading and Writingscores using your practice test’s raw score conversion table. Find your raw scores for each section and then look across to the corresponding column to determineyour Reading and Writing test scores. These test scores, though scaled, are not your final section scores.Unlike PSATsectionscores, which use a score range of 160-760, test scores use a much smaller rangeof 8-38. Myraw Reading score above was 34, and my raw Writing score was 38. According to the following conversion table, these two raw scores convert into scaled (test) scores of30 and 33, respectively: Raw Score Reading Test score Writing and Language Test Score Raw Score Reading Test Score Writing and Language Test Score 0 8 8 24 25 25 1 9 9 25 26 25 2 10 10 26 26 26 3 27 27 27 4 12 12 28 27 27 5 14 13 29 28 28 6 15 14 30 28 28 7 16 14 31 29 29 8 16 15 32 29 29 9 17 15 33 30 30 10 18 16 34 30 30 18 16 35 31 31 12 19 17 36 31 32 13 19 18 37 32 32 14 20 18 38 32 33 15 20 19 39 33 34 16 21 20 40 34 35 17 21 20 41 34 36 18 22 21 42 35 37 19 22 21 43 36 37 20 23 22 44 37 38 21 23 23 45 37 22 24 24 46 38 23 24 24 47 38 Step 3: Combine for Total Score Once you have your individual Reading and Writing test scores, combine these scores to get a total EBRW test score on a scale of 16-76. Finally,multiply this sum by 10 to get your scaled EBRW score. As an equation, this conversion process can be writtenas so:(R+W)10=EBRW. In my example above, my Reading and Writing test scores were 30 and 33, respectively. Using this equation, then, here's what my EBRW score comes out to: (30+33)10=(63)10=630. Now,add your EBRW section score to your Math section score to getyour total PSAT score out of 1520. Inmy example, my total PSAT score would be650+630=1280. How to Calculate PSAT Subscores and Cross-Test Scores In addition to calculating your raw and scaled scores, you have the option ofcalculating your subscores and cross-test scores. These additional scores offer a closer, more detailed analysis of your performance on particularcontent areas and question types on the PSAT. Read on to learn how to calculate PSAT subscores and cross-test scores. Subscores To calculate your subscores, start by finding your raw scores for each of the following subscore categories: Math Heart of Algebra Problem Solving and Data Analysis Passport to Advanced Math EBRW Expression of Ideas Standard English Conventions Words in Context Command of Evidence Add up your correct answers on Math and EBRW using their respective answer keys. Then,use your scoring guide to see which questions on your test make up whichsubscore categories. Here is an example of a subscore overview for the EBRW subscore Expression of Ideas: Once you’ve got your seven raw subscores, use your test’s raw score conversion table for subscores to convert your raw subscores into scaled subscores. All scaled subscores use a scale of1-15. So forexample, if I were to get a raw score of 17 on Expression of Ideas, my scaled subscore would be12: Unfortunately, you're not allowed to have a lab partner on science questions. Cross-Test Scores You’ll also receive two cross-test scores: Analysis in History/Social Studies Analysis in Science Unlike subscores, cross-test scores are notconfined to a single section on the PSAT. This means that you can find a combination of Analysis in History/Social Studies and Analysis in Science questions in both the EBRW and Math sections. Each cross-test score begins as a raw score. To find your raw cross-test scores, use your scoring guide to determine which EBRW and Math questions make upwhich cross-test categories. Below is an example of a cross-test score overview for the Analysis in Science score: Once you have your raw scores for both cross-test scores, use your test’s raw score conversion table for cross-test scores to figure out your scaled cross-test scores for History/Social Studies and Science. Scaled cross-test scores use a scale of 8-38 (note that this is different from the 1-15 scoring scale used for subscores). Soif I were to receive a raw score of 19 on Analysis in Science, my scaled cross-test score for that area would equal 29: How to Calculate National Merit Selection Index Finally, there’s the National Merit Selection Index score. Unlike the other scores we’ve covered so far, you won’t find any conversion table for your Selection Index ona PSAT practice test. So how can you calculate this score? Here are the steps to take: 1. Find your Reading and Writing test scores. To find these scores, calculate your raw scores for Reading and Writing and then use your raw score conversion table to convert your raw scoresinto scaled testscores (on a scale of 8-38). 2. Find your Math test score. Unlike your Reading and Writing scores, your Math test score isn’t on a conversion chart. So how do you find this score? First,get your Math section score by matching your raw Math score to its corresponding scaled score on your conversion table. Then, to get your Math test score, simply divide your Math section score by 20. So ifmy scaled Math score were 680, my Math test score would be 680/20=34. 3. Add your test scores together. Next, combine your Reading, Writing, and Math test scores. This will give you a total PSAT test score on a scale of 24-4. 4. Multiply your total test score by 2. Finally, take your total PSAT test score and multiply it by 2 to get your Selection Index. Once again, the Selection Index score range is 48-228. In the end, if you’re aiming for a scholarship, you’ll need to have a Selection Index high enough to qualify you for National Merit in your particular state. These cutoff Selection Index scores range anywhere from 209-222. For more information about the Selection Index scores needed to qualify, check out our guide on how to become a National Merit Semifinalist. Want to improve your PSAT score by 150 points? We have the industry's leading PSAT prep program. Built by Harvard grads and SAT full scorers, the program learns your strengths and weaknesses through advanced statistics, then customizes your prep program to you so that you get the most effective prep possible. Check out our 5-day free trial today: Next up, we'll decipher the meaning of PSAT score calculations. What Do PSAT Score Calculations Mean for YOU? So far we’ve explained how to calculate various PSAT scores, from raw and scaled scores to subscores, cross-test scores, and Selection Index scores. But what do all of these calculations mean for you? Using conversion tables as a PSAT score calculator allows you to forma rough idea as to how many questions you’ll need to answer correctly in order to attain a certain scaled PSAT score. Essentially,if you have aPSAT goal scorein mind, you can use raw score conversion tables from official PSAT practice tests to estimate how many correct answers you’ll need to be able to hit your goal score on test day. For example, let’s say your total PSAT goal score is 1300, or 640 on Math and 660 on EBRW. To get 640 on Math, you’ll need to scorearound 34-38 raw points, or get 34-38 questions right. (We calculated this estimated raw score range using the official conversion tables for PSAT Practice Test #1 and #2.) Figuring out the number of questions you'll need to get right for EBRW, however, requires you to do more than just look at a conversion table. You'll first need to divide your EBRW goal score (in this case, 660) by 10 to get your EBRW test score. Then, divide this score by 2 to get your estimated test scores for the Reading and Writing sections. Finally, use official conversion tables to get a corresponding raw scorefor each of these two test scores. In my example, a 660 EBRW goal score equals about 38-39raw points for Reading and 37-38 raw pointsfor Writing. Of course, these raw score ranges are all simply estimates. Because the College Board doesn’t tell us ahead of time how raw scores for upcoming PSATs will be equated, there’s no way to know for sure how many questionsyou’ll need to answer correctly in order to hityour goal scores. Still, you can get a pretty close approximation using official conversion tables! Recap: How to Calculate PSAT Score The PSAT is scored on a scale of 320-1520 in 10-point increments. This total score consists of two section scores for Math and EBRW, each of which uses a scale of 160-760. You’ll also getsubscores on a scale of 1-15 and cross-test scores on a scale of 8-38. Lastly, you’ll get a Selection Index score on a scale of 48-228; this score's sole purpose is todetermine your eligibility for National Merit. All of these PSAT scores are scaled, or equated, scores. Your PSAT scores will start out as raw scores based on the number of questions you answered correctly. Yourraw scores are then converted into scaled scores using a special equating process exclusive to yourtest. To convert your raw scores into scaled scores (or even vice versa), useraw score conversion tables for official PSAT practice tests. Though these tables apply to specific practice tests only, you can use them as a convenient PSAT score calculator toestimate the number of questions you’ll need to answer correctly in order to hit your goal scores on test day. What’s Next? Want to learn more about PSAT scoring and the PSAT score range? Our in-depth guides explainhow the PSAT score range differs from the SAT score range as well as how you can use the PSAT scoring system to your advantage. Are you aiming for National Merit?Get the rundown on how to win a scholarship and what you can do to guarantee yourself a perfect PSAT score! Want to improve your SAT score by 160 points or your ACT score by 4 points?We've written a guide for each test about the top 5 strategies you must be using to have a shot at improving your score. Download it for free now:

Improving Maternal health Research Paper Example | Topics and Well Written Essays - 1750 words

Improving Maternal health - Research Paper Example Despite maternal health concern being in the millennium development goals, the condition is still wanting. Maternal has for been a leading cause of death for many women and children. Efforts have been made to handle the situation with political aid. According to world health organization report of 2012, it has led to the global reduction of maternal health by 47% since 1990 to 2012. However, approximately 800 women die daily from preventable causes related to pregnancy and childbirth. In most underserved and marginalized communities are unable to access the information, resources, and services leading to prevailing of poor maternal health. Filippi demonstrated the health condition in developing countries to be poor compared to the developed countries (361). The factors that drive communities to high mortality rates despite the measure put to control are variety. Poverty, lack of knowledge, cultural ties, few skilled attendants and distance to hospitals are contributing factors to mor tality deaths. There is a need to look into the issue deaths related pregnancies to safeguard the lives the mother and the child. WHO report of 2013 suggested an estimation of 289,000 women died during delivery. According to Bergsma, the situation in developing countries is 97 times worse than in developing countries. Antenatal care would reduce maternal mortality (35-54). The majority of deaths are reported to occur during and immediately following birth. WHO â€Å"Maternal Mortality† report shows that excessive bleeding causes 25%, 15% due to infections, 12% for the seizure disorder and 8% are due to obstructed labor. Other causes of death during pregnancy include unsafe abortions that account for 13% of the total deaths. The situation is so alarming in the society and needs further actions to reduce the deaths globally. The issue of death is extended to the postpartum period.  

Business Law Essay Example | Topics and Well Written Essays - 1750 words - 2

Business Law - Essay Example What will happen if people will know about the duplication? Will there be legal consequences given the situation? Brief Answer One of the possible effects of what Sam Evening’s act is getting charged of theft by false pretenses. This includes false promises which are promises without intent of performance. In the case at bar, Sam Evening and Janet Evening promised to sell to the customers 1000 pieces of Limited Royal Wedding Collectibles which are handmade and personally painted and signed by the artist. The customers are being promised with the quality and the worth of the product. But selling a product made through the service of duplication company is making false pretenses and future promises about products. They are selling the products with intention to gain. Courts will require having a good materiality of misrepresentation. There should be causal relation between the swindler’s deception and the victim’s loss. The state of mind of the accused with respect to his intentions should be given great importance. In the case, Sam’s situation can be said to be a form of obtaining money by false pretenses. Another possible legal effect of Sam’s action is theft by deception. A different offense and can be define in a broader sense. This is the type of theft which uses deception to obtain property of another or service of another. This happens when a person has an intention to deceive other persons to gain. Sam Evening will also be held liable for damages under the Tort Law. These are the damages that he will eventually cause to his business partners under breach of partnership trust. Under the Tort Law, a relief is provided for those who suffered harm from the wrongful acts of others (Hg.org, Tort Law). Statement of Facts The case at bar is considering the possible legal issues that Sam Evening will face after selling products made through the service of duplication company. The products are to be sold as Limited Edition Royal W edding collectibles. There will only be 1000 limited collectibles to be sold for $100. Janet and Sam are so confident that the plates would increase in value. The sellers decided to guarantee the increase in value by promising to buy any plate back within five years from issuance at an appreciated price of 5% annually. Sam and Janet and a friend of theirs, Largess Bucks, each contributed $1000 to cover expenses Sam began producing and signing the plates and Janet created a website to advertise and sell the plates to customers in the United States. After handpainting, signing and numbering 37, Sam got tired and felt like he was doing all of the hard work. Janet did manage the website, including processing payments and shipping products. Their other partner is Largess did nothing. Sam Evening found a plate duplication service and decided to get the service of a duplication company to finish the works of the plates. The company required a minimum order of 1000 plates in order to perfor m these services and a down payment of $3000 to start the order with the remaining $7000 to be paid upon delivery. Unfortunately of the $3000 that they had contributed, $1000 had been used for initial supplies, $500 to set up the website payment processing service, $185 for initial shipping supplies and $315 had been paid to repurchase three plates out of a total of ten plates that had been shipped so far. Sam thought that income from the first set of plate sales would be given at the end of April. So Sam decided to take the $1000 remaining and added $1000 of his

Hydrophobic And Hydrophilic Interaction In Protein Folding Biology Essay

Hydrophobic And Hydrophilic Interaction In Protein Folding Biology Essay Review the mechanism of protein folding Module: Enzyme Technology and Biocatalysts Module leader: Prof. Steve Forsythe Proteins are the bio molecules which play pivotal role in this living world. They are responsible for expression of certain characters in different types of cells and constitute around 50% of the total cell dried mass. Proteins are the chain of amino acids which binds with polypeptide backbone and then fold in a unique 3D (native) structure by which protein expression takes place. Various forces and factors are responsible for protein folding .If right expression of the protein will not take place, it will cause disorders in human body. Many diseases like Alzheimers; Parkinson, cystic fibrosis etc (Baldwin 2007) is caused due to improper folding of proteins. For proper expression of protein, the amino acid chain should be in its unique 3D structure. Sometimes proteins require assistance in folding, molecules which help in the folding are known as chaperones. These molecules help in the folding of the certain protein molecules and also prevent the unfolding of the molecules. In this assignment, I have tried to describe the mechanism of the protein folding and effect of various factors which influence protein folding by taking into consideration the present developments in our understanding of thermodynamics and kinetics of protein. INTRODUCTION Protein folding refers to the process by which a protein assumes its characteristic structure, known as the native state. Protein folding is very complex mechanism and great development in its understanding has been achieved in last 20years due to the development and use of some sophisticated modern techniques like X Ray Crystallography, N.M.R, and Mass Spectrometry etc. In the last few decades, we have managed to find the 3D structure of various proteins and how actually protein folding takes place. In the complex process of protein folding, various factors act together to construct specific 3D structure of a protein. Protein folding is a very quick process taking milliseconds to seconds. Due to high speed of folding, it is not possible to find each and every possible conformation in fractions of time. Levinthal stated that each protein can possibly have millions of pathway by which a desired 3D pattern can be achieved. By study of intermediates we can understand the mechanism or pattern on which protein folding works. But it is impossible to find out all possible structure of protein molecules. Protein folding study uses denaturants which help to denature the protein. The logic is to use denaturing conditions viz. high pH, Temp, Pressure etc to stop folding at intermediate stages (Stop flow technique) to study these intermediates, thereby generating an overview of the whole process. Fully folded structure is also known as native structure. Protein folding studies have also been done in in-vivo and in-vitro conditions. In in- vivo protein folding, some metal ions act as cofactors. These cofactors stabilise and accelerate protein folding and finally help to achieve native stage .Macromolecules like chaperones initiate protein folding, helping the protein molecule to retain its folded confirmation and making it stable. In-vitro concentration of macromolecules is very less, around 1% of what is originally present in the cell. So inside cell, these molecules also affect protein stability and make them more stable than in vitro (Rumfeldt et al. 2008) Protein folding can be a two stages or multistage process, depending upon the type of sequence. A single point mutation can change folding from two stages to multistage and vice-versa .Some previous studies show that protein sequences of less than 80 amino acids prefer two stage folding and large protein sequences having more than 130 amino acids prefer multi stage folding. Later studies have shown that sequences rich in F and G amino acids prefer two stages folding where as sequences rich in C, H, L and R amino acids prefer multistage folding (Ma, Chen Zhang 2007) PROTEINS FOLDING Hydrophobic and hydrophilic interaction Proteins are made of amino acids and joined by polypeptide bonds leads to formation of polypeptide backbone. We have only 20 type of the amino acids .whose combinations code for such complex structure and folding .These amino acids can be divide in two groups one is hydrophilic or polar group and other is hydrophobic or nonpolar group and their interaction with the cytoplasm make them folded(Trevino, Scholtz Pace 2007) POLAR OR HYDROPHILIC AMINO ACID NON-POLAR OR HYDROPHOBIC AMINO ACID ASPARTIC ACID D ALANINE A GLUTAMIC ACID E GLYCINE G ARGNIN R VALINE V LYSINE K LEUCINE L HISTIDINE H ISOLEUCINE I ASPARAGINE N PROLINE P GLUTAMINE Q PHENYLALANINE F SERINE S METHIONINE M THREONINE T TRYPTOPHAN W TYROSENE Y CYSTEINE C In the early stages of research, problem was why protein folds to a specific structure and which part of the protein carried information for the folding and later on this was find that primary structure of the protein code for the final 3D structure. Hydrophilic and hydrophobic interactions of the amino acids adjust protein it such a way that it suffers minimum repulsion and problem from the surrounding. In folded state of protein all hydrophilic amino acid molecules come at the other side and interact with water in the cytoplasm and hydrophobic molecule come at the inner side of the molecule and dont show any reaction and attraction with water molecules and ultimately protein folding take place in such a way that suffer minimum repulsion (Baldwin 2007) All amino acids have different energetic in secondary structure. There are many chameleon sequences in protein structure which can be taken as alpha helix or beta sheets depending upon the tertiary structure of protein. These chameleon are stabilised by hydrophobic forces (Chen et al. 2008) Fig.a shows yellow colour hydrophobic molecules inner side of structure Fig.b shows folding takes place and keeps hydrophobic molecules in inner side (Chen et al. 2008) Apart from these interactions hydrogen bonding is very important in the protein folding. Hydrogen bonding takes place between hydrogen and electronegative atoms In the maintenance of the native structure hydrogen bonding present in between the polypeptide amino acid chain which helpful in the formation of the secondary, tertiary and quaternary structure of the proteins. Hydrogen bonding also interacts between polar and side chain residues with the surrounding water molecules. During the denaturing of the protein hydrogen bond between protein molecules break and native structure of protein disturbed (Djikaev, Ruckenstein 2010) Hydrophobic interactions are also responsible for the protein folding. During hydrophobic interactions amino acids which are non polar or hydrophobic they align themselves in such a way that all hydrophobic come together and all hydrophilic molecules make hydrogen bonds with water molecules, all hydrophobic amino acid come in to inner side of the protein molecules and formation of the nuclei take place which is hydrophobic these interaction further helpful in the secondary, tertiary structure and due to this protein sta bilise and help to achieve native structure because hydrophobic molecules will not interact with water and always have repulsive attitude toward water and let the protein in the folded form and finally such type of the folding take place in which molecule have hydrophobic core and all hydrophilic molecules in periphery of the folded structure(Berezovsky et al. 2001) Free energy and entropy (G, E) Gibbs free energy (G) is also defined as the amount of the energy which is free and this can also be defined as the measure of unstableness and this measured by simple equation G= H-TS G=free energy, H=enthalpy, S=entropy, T= temperature Entropy (S) is defined as degree of randomness in any system, in terms of protein folding this can be define as the measure of the possible structure in the protein molecule at that value of the entropy. Entropy is responsible for the possible out come of protein as much high would be entropy as much high number of the confirmation would form. To minimise the entropy in the protein folding various force come in play like hydrogen bonds, salt bridges, disulphide bonds etc. these bonds help to reduce the entropy and favour protein folding(Brady, Sharp 1997)BOLTZMANN worked on the entropy and give us a very useful relation between atomic theory and entropy. Boltzmann proposed an equation which shows that entropy in any unfolded protein structure is equal to the product of his constant(KB) and natural log of number of all possible states which any protein can adopt(S) S = KB * NATURAL LOG (S) KB=Boltzmann constant Protein folding prefers low value of entropy and follows that smallest path in which value of entropy is low. At different value of the entropy different number of structure could be present and finally all structure will vanished and one structure would be present at the minimum value of entropy, which is our native structure (Weikl, Dill 2003) Enthalpy (H) is also responsible for protein folding. This is also known as the measure of the total energy of the system including internal energy (U). P and V are the pressure and volume of system H= U+P*V So, we should search for such structure which have low value of enthalpy then the free energy, because which structure have low value of enthalpy that will have low value of free energy too(Brockwell, Smith Radford 2000) Gibbs free energy equation is the single solution for all protein folding problem. Gibbs equation shows that in case of protein folding, stable state will have minimum value of G. unfolded state have higher free energy then the folded one and protein folding have many intermediates, This stage is less populated stage and have maximum energy in the whole system, all above mention factor in the Gibbs equation adjust and finally provide such folded state in which value of G is minimum and this is known as fully folded and stable confirmation(Finkelstein, Badretdinov 1997) (www.biology-online.org/articles/statistical_thermodynamics_taking_walk.html) Chaperones Chaperones are bio molecules which participate in the protein folding. Proteins need assistance in the folding and binds with cofactors .which allow them to fold properly .these cofactor known as chaperones. These chaperones bind with the protein as N terminus of the protein formed and leave ribosome and until and unless protein gain his fully active 3D state and become functional(Tomala, Korona 2008) Chaperones are not only helping in the correct protein folding but they also help protein to maintain its correct 3D structure and prevent them to unfold .these molecules comes in to play when cell is under stress due to favourable conditions are not present and they also known as the H.S.P (heat shock protein).these molecular chaperones are HSP40(Dnaj), HSP60(GroEl), HSP70(Dnak) etc.(Rikhvanov, Romanova Chernoff 2007) Copied from Yon, Betton 1991 Mode of action Chaperones recognise non native protein structure by their exposed hydrophobic regions Chaperones action is driven by ATP and for the activity of the chaperones assistance protein folding need of energy, which is provided by the ATP. These chaperones bind with the intermediate and unfolded protein structure by the utilisation of the ATP intermediates or random coil structure are unfolded and again they are fold in the correct 3D structure (NATIVE structure). Chaperones molecules are task specific that are different molecules perform different functions. For example: HSP70/40 They prevent aggregation and misfolding of newly synthesised protein molecules. HSP60 They unfold intermediate and then fold them properly in to native structure Chaperones are like catalyst, they enhance rate of protein folding and assist protein folding to native structure and after the formation of the native structure they separated. As like catalyst they required energy for the initiation of the process Chaperones activity is much specialised, in stress condition protein get mutated, denature, and aggregate. Which may cause some wrong expression and code for some disease .In such situations they are enough capable to provide personalised treatment to different protein (Yon, Betton 1991)They can easily point out that which protein intermediate structure need to be degraded and which protein intermediate to be stabilise in the native structure and path should be follow for this process. In some mutation destabilise protein can be easily stabilized by HSP70 and some over expression of the specific chaperones. For example: In bacteria HSP70 bind with the protein polypeptide chain during translation after the synthesis some protein released for expression and some may attached for some specialised folding and most destabilise polypeptide chain degraded by chaperones (Tomala, Korona 2008) Chaperones activity is not simple they have multiple steps in their folding mechanism. Some chaperones required some other chaperones intermediate as substrate and then they provide native structure. Hsp90/70 mechanism chain Some chaperones may responsible for disease. it has been found that HSP90 enhance cancer development because many mutated protein mature in the presence of the HSP90 and cause cancer , repressing HSP90 such type of cancer can be able to prevent but problem associated with this is due to this action some non mutagenic protein will be degrade and not express and cause problem. But on other side HSP70 acts as good repressor in neurodegenerative disease and prevent this disease in the fruit flies (Tomala, Korona 2008) Models of protein modelling and structure prediction Plaxco and co-worker model: This model shows that high degree of correlation between folding rate and structural properties of protein explain on the basis of contact order (CO). This can be cross validated from various experiments that folding rate and contact order are dependent to each other. ,    L  is the sequence length   N  is the total number of inter-residue atomic contacts   ÃƒÅ½Ã¢â‚¬ Lij  is the sequence separation of contacting residues  i  and  j Kuznetsov and rackovsky showed that structural based determinants can serve as good determinants of folding rate and many other researchers searching for which structural and sequence based determinants can serve as unique predictor of folding rate (Shakhnovich 2006) Dokholyan and co-workers model: They use simple protein model and find out transition state of src homology 3(SH3) to find out contribution of each amino acid in transition state. They calculate ÃŽÂ ¦ value and on this basis they find high correlation between simulation and experimental ÃŽÂ ¦ value .in the end of their experimental model they conclude that L24 and G24 are two most important residues in the folding of proteins Physics and bioinformatics based models: Physics models are very helpful to understand protein folding rate and route to folding. These physics based models help to understand the various forces and their dynamics in protein folding. These models help to understand: Conformational changes in protein Mechanism of folding, enzyme catalysis, mode of action protein Response to ph salt and denaturants(Brockwell, Smith Radford 2000) Bioinformatics is very important tool to find out the structure and folding pattern of the protein molecules. In this we add our computer based program along with these physics model and within the fraction of time provide us 3D structure of protein. Various databases on web are present which contain information regarding proteins only like NCBI, PUBMED etc. these databases contain all information about proteins by the comparison of our unknown sequence using bioinformatics tools with these databases we can find out possible structure and folding pattern and helpful in drug discovery, possible remedy against disease etc. Now, how collectively these factors works After having the knowledge of these factors now we can easily understand how they act and result to the fully folded 3D structure. Primary structure of protein code for 3D structure and all above factors participate to provide a functional unit. initially primary structure of protein are made of different type of amino acids on the poly peptide back bone and just after the production of the N-terminus protein folding starts and secondary structures alpha helix and beta sheets are formed. In alpha helix all amino acid chain remain in the periphery of the helix and this structure formed due to hydrogen bonding and di-sulphide bonding (Trevino, Scholtz Pace 2007) After the formation of secondary structure, tertiary structure these hydrophobic interaction, hydrogen bonding and charge on the molecule come it to the play now this protein molecule structure fold in such a way to minimise all these forces and try to give an stable confirmation to protein(Chen et al. 2008) Free energy and entropy act simultaneously. After attachment of these secondary structures stability is not uniform in the whole tertiary structure. There may be possibility that two stable structures are joining by unstable and less stable strands and in that case folding take place in such a way to minimise the free energy of the system. This type of stage is known as the intermediate stage. In this stage all amino acids are attached in the structure but the entropy of the system is high and due to which this show high presence of free energy and may have the millions of the possibilities of the intermediate structure. Now protein starts folding from intermediate to the stable or native structure by minimising the interaction between the molecules. Due to which all the hydrophobic or non polar amino acid come in the centre of the structure and the formation of hydrophobic core take place of 3D structure and all polar or hydrophilic molecules come at the periphery of the 3D structur e(Chen et al. 2008). Out of millions of the possibilities there are many path which favour this folding in term of having minimum energy and protein molecule select that path which is shortest and this may contain several steps in folding and ultimately leads to the formation of native 3D structure Copied from Ma, Chen Zhang 2007 There is always some equilibrium in some folded and intermediates state and molecules may be aggregate. this depend upon the pH, Temp, Pressure and denaturation agents and the protein structure destabilise it start affecting other native protein structure in this stage chaperones act as cofactors and help in the and maintaining native structure of protein(Ma, Chen Zhang 2007) SUMMARY In the protein folding 3D structure of protein plays an important role in the protein expression and their function. Information regarding protein folding is present in the primary structure of the protein which bioenergetics can be determined by bound amino acid. Hydrophobic forces play an important role. They all concentrate at the centre of the molecules and hydrophilic at the periphery of the structure. Hydrogen bonding plays an important role due to which all polar molecules bound with the surrounding medium in cell and makes protein molecule structure rigid and compressed. Protein folding is a spontaneous process in which entropy of the molecule is decreasing and finally provides a folded structure. Protein native structure must have low value of Gibbs free energy, entropy, and enthalpy and lower the value, higher will be the degree of protein stability. Protein may unfold due to the presence of the unfavourable condition like temp, pressure, pH, and denaturing agent. In such a case special type of molecules help in the folding known as chaperones and helpful in maintaining native structure of protein.

Lord of the Flies – How is the idea of the beast developed?

The idea of a beast on the island emerges early in the story, which quickly evolves from the imagination of one little boy. At first the idea is superficially rejected but subconsciously absorbed and as a result it continues to develop. The concept of a dangerous presence on the island originates when one of the children mentions he has seen a â€Å"snake – thing. Ever so big†¦Ã¢â‚¬ ¦.in the woods, † an idea which is quickly dismissed by the older boys as part of his imagination. Soon, many of the older boys begin to wonder about the existence of some kind of beast, and although many were not willing to admit this, its fear was demonstrated by their horrible nightmares and night screams. Later, talk of beasts emerges at an assembly where the vast majority agreed on its presence on the island and although Simon had already figured out that this idea came from their inner fear, he was not able to get this point across. Orwell reveals the reader, through Simon, how the creation of the beast is used to take the blame for all the chaos and disasters. Furthermore, the creation of the beast is just an excuse to believe the cause of evil is due to it, not to them. As a result, it becomes critical to find a definite shape for the beast and prove its existence as this would automatically release them from the guilt the evil emitted. Soon after, a dead parachutist's corpse is confused with the beast, and the children become convinced of the existence of the beast. In a later assembly, Jack decides to leave the group as he refuses to obey more rules. Many others decide to follow him, as they felt more secure with him. The idea of the existence of the beast gave Jack control over the other children. The concept of a beast is allowed to develop due one main reason; fear. Fear of the unknown, together with the children's imagination, built up the idea of a beast inhabiting the island. Yet, many other factors contribute to its development, such as Jack's desire for control. Throughout this novel, the boys are constantly faced with various fears, yet nothing compares to the fear they feel towards the beast. The beast represents how human beings will try to convince themselves that evil is not present inside them, by making someone or something else seem to be the cause for the evil. The beast is a metaphor used to demonstrate how the imagination can be manipulated to let it grow; à ¯Ã‚ ¿Ã‚ ½The beast had teeth, à ¯Ã‚ ¿Ã‚ ½ said Ralph, à ¯Ã‚ ¿Ã‚ ½and big black eyes.à ¯Ã‚ ¿Ã‚ ½ Yet Golding's purpose in developing the concept of the beast was to demonstrate the connection between evil and fear, to show us that fear is the thought and evil is the reaction, as it is proved by the murder of Simon, when he was confused with the beast which inhabited in their minds.

The Ethical Dilemma Of Bangladesh - 1765 Words

Problem Recognition/Ethical Dilemma Repeated disasters due to poor work conditions has raised concern for everyone around the globe. These disasters have everyone wondering when will someone step up to make a change so that these occurrences will not continue to happen to the struggling people of Bangladesh. Outsiders feel as if the retailers who use Bangladesh garment industry should start doing more to ensure work conditions are safe for employees of the factories. Mr. Sohel Rana, the owner of Rana Plaza, should be responsible for all decisions concerning Rana Plaza. He should be the one to step up and cease operations of the plaza until work conditions improved. He was aware of the work conditions, but he insisted that they were†¦show more content†¦The country of Bangladesh as a whole and employees in these textile factories has the most to gain in the outcome of improved work conditions and higher wages for employees. Better working conditions will allow for the factori es to continue operations which will generate income for the country and grow the economy. Employees of the factories will live a more fluent life with an increase in wages. Employees will also accomplish more without having to be concerned about their safety and whether they will make it home to their families or not. Identification and Evaluation of Possible Alternatives There are a wide array of alternatives that could be put in place to improve the work conditions in the factories in Bangladesh. A governing board can be created comprising of leaders from retailers who use the factory, representatives from the United Nations International Labor Organization, and political leaders in the United States, Europe, and China. This will allow for the leaders from the retailers to get a first-hand look at the work conditions in the factories. 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