- The primary sequence of a protein is linked together using dehydration synthesis that combine the carboxylic acid of the upstream amino acid with the amine functional group of the downstream amino acid to form an amide linkage. Within protein...Link: https://unix.com/shell-programming-and-scripting/274308-mailx-attachment-html-content.html
- Thus, proteins are always synthesized in a directional manner starting with the amine and ending with the carboxylic acid tail. New amino acids are always added onto the carboxylic acid tail, never onto the amine of the first amino acid in the...Link: https://quizlet.com/384289589/nurs-2300-uta-exam-2-blueprint-gen-edition-flash-cards/
- There are a total of 20 alpha amino acids that are commonly incorporated into protein structures Figure Due to the large pool of amino acids that can be incorporated at each position within the protein, there are billions of different possible protein combinations that can be used to create novel protein structures! For example, think about a tripeptide made from this amino acid pool. At each position there are 20 different options that can be incorporated. Thus, the total number of resulting tripeptides possible would be 20 X 20 X 20 or , which equals 8, different tripeptide options!Link: https://pacificmedicalacls.com/ovtest2answers.html
- Now think about how many options there would be for a small peptide containing 40 amino acids. There would be options, or a mind boggling 1. Each of these options would vary in the overall protein shape, as the nature of the amino acid side chains helps to determine the interaction of the protein with the other residues in the protein itself and with its surrounding environment. Thus, it is useful to learn a little bit about the general characteristics of the amino acid side chains. The different amino acid side chains can be grouped into different classes based on their chemical properties Figure For example, some amino acid side chains only contain carbon and hydrogen and are thus, very nonpolar and hydrophobic. Others contain electronegative functional groups with oxygen or nitrogen and can form hydrogen bonds forming more polar interactions. Still others contain carboxylic acid functional groups and can act as acids or they contain amines and can act as bases, forming fully charged molecules.Link: https://youtube.com/watch?v=EZzjvnCO33M
- The character of the amino acids throughout the protein help the protein to fold and form its 3-dimentional structure. It is this 3-D shape that is required for the functional activity of the protein ie. For proteins found inside the watery environments of the cell, hydrophobic amino acids will often be found on the inside of the protein structure, whereas water-loving hydrophilic amino acids will be on the surface where they can hydrogen bond and interact with the water molecules. Proline is unique because it has the only R-group that forms a cyclic structure with the amine functional group in the main chain. This cyclization is what causes proline to adopt the cis conformation rather than the trans conformation within the backbone. This shift is structure will often mean that prolines are positions where bends or directional changes occur within the protein. Methionine is unique, in that it serves as the starting amino acid for almost all of the many thousands of proteins known in nature.Link: https://youtube.com/watch?v=eHQw9ZpXJkU
- Cysteines contain thiol functional groups and thus, can be oxidized with other cysteine residues to form disulfide bonds within the protein structure Figure Disulfide bridges add additional stability to the 3-D structure and are often required for correct protein folding and function Figure Disulfide bonds are formed between two cysteine residues within a peptide or protein sequence or between different peptide or protein chains. In the example above the two peptide chains that form the hormone insulin are depicted. Disulfide bridges between the two chains are required for the proper function of this hormone to regulate blood glucose levels.Link: https://home.pearsonvue.com/bcen
- Protein Shape and Function The primary structure of each protein leads to the unique folding pattern that is characteristic for that specific protein. Recall that this is the linear order of the amino acids as they are linked together in the protein chain Figure These specific motifs or patterns are called secondary structure. Common secondary structural features include alpha helix and beta-pleated sheet Figure Within these structures, intramolecular interactions, especially hydrogen bonding between the backbone amine and carbonyl functional groups are critical to maintain 3-dimensional shape.Link: http://csg.csail.mit.edu/6.175/labs/lab1-multiplexers-adders.html
- Every helical turn in an alpha helix has 3. The R groups are attached to the carbons and extend above and below the folds of the pleat. The pleated segments align parallel or antiparallel to each other, and hydrogen bonds form between the partially positive nitrogen atom in the amino group and the partially negative oxygen atom in the carbonyl group of the peptide backbone. The alpha helix and beta-pleated sheet are common structural motifs found in most proteins. They are held together by hydrogen bonding between the amine and the carbonyl oxygen within the amino acid backbone. The most highly traveled and culturally significant of these was called the Silk Road. The reason that the Silk road was so culturally significant was because of the great distance that it covered. Essentially the entire ancient world was connected by one trade route. The silk road had an astounding effect on the creation of many societies. It was able to bring economic wealth into areas along the route, and new ideas traveled the distance and influence many things including art.Link: https://arzhanghome.com/dru5nvxxu/cb7dniu6kfemjpn.php?up=5&et=135&jjqg=2021st&xcwbz=amsco-chapter-16-notes
- An example of this is Buddhist art that was found in India. The painting has many western influences that can be identified in it, such as realistic musculature of the people being painted. Also, the trade of gun powder to the West helped influence warfare, and in turn shaped the modern world. The real reason the Silk Road was started though was for the product that it takes its name from: Silk. The Silk showed that the rulers had power and wealth because the silk was not easy to come by, and therefore was definitely not cheap.Link: https://link.springer.com/chapter/10.1007%2F978-3-319-54930-9_24
- Silk was first developed in China, and is made by harvesting the silk from the cocoons of the mulberry silkworm. The silk itself is called a natural protein fiber because it is composed of a pattern of amino acids in a secondary protein structure. The secondary structure of silk is the beta pleated sheet. The primary structure of silk contains the amino acids of glycine, alanine, serine, in specific repeating pattern. These amino acids are used as side chains and affect things such as elasticity and strength. The beta pleated sheet of silk is connected by hydrogen bonds. The hydrogen bonds in the silk form beta pleated sheets rather than alpha helixes because of where the bonds occur. The hydrogen bonds go from the amide hydrogens on one protein chain to the corresponding carbonyl oxygen across the way on the other protein chain. This is in contrast to the alpha helix because in that structure the bonds go from the amide to the carbonyl oxygen, but they are not adjacent.Link: https://ihu.edu.tr/en/undergraduate-programs-registration-guide/
- The carbonyl oxygen is on the amino acid that is four residues before. The formation of this secondary structure in the silk protein allows it to have very strong tensile strength. Silk also helped to form one of the greatest trading routes in history, allowing for the exchange of ideas, products and cultures while advancing the societies that were involved. Silk contains both anti-parallel and parallel arrangements of beta sheets. In consequence very bulky side chains make the structure unstable. This explains why silk is composed almost entirely of glycine, alanine, and serine, the three amino acids with the smallest side chains. The complete 3-dimensional shape of the entire protein or sum of all the secondary structures is known as the tertiary structure of the protein and is a unique and defining feature for that protein Figure Primarily, the interactions among R groups creates the complex three-dimensional tertiary structure of a protein.Link: https://emsnav.com/mca-courses/mca-approved-engine-course-2-aec2.html
- The nature of the R groups found in the amino acids involved can counteract the formation of the hydrogen bonds described for standard secondary structures. For example, R groups with like charges are repelled by each other and those with unlike charges are attracted to each other ionic bonds. When protein folding takes place, the hydrophobic R groups of nonpolar amino acids lay in the interior of the protein, whereas the hydrophilic R groups lay on the outside. The former types of interactions are also known as hydrophobic interactions.Link: https://brainscape.com/flashcards/csw-practice-test-1053295/packs/1945190
- Interaction between cysteine side chains forms disulfide linkages in the presence of oxygen, the only covalent bond forming during protein folding. The tertiary structure of proteins is determined by a variety of chemical interactions. These include hydrophobic interactions, ionic bonding, hydrogen bonding and disulfide linkages. All of these interactions, weak and strong, determine the final three-dimensional shape of the protein. When a protein loses its three-dimensional shape, it is usually no longer be functional. In nature, some proteins are formed from several polypeptides, also known as subunits, and the interaction of these subunits forms the quaternary structure. Weak interactions between the subunits help to stabilize the overall structure. For example, insulin a globular protein has a combination of hydrogen bonds and disulfide bonds that cause it to be mostly clumped into a ball shape.Link: https://chegg.com/homework-help/questions-and-answers/test-midterm-exam-time-remaining-01-38-25-submit-test-question-5-pts-9-10-o-complete-test--q72530890
- Insulin is produced and stored in the body as a hexamer a unit of six insulin molecules , while the active form is the monomer.Link: https://coursehero.com/file/71407045/NAHQ-POST-TEST-pdf/
- Is rust a mixture, compound or element? When atoms combine products of a chemical reaction they form what? Can you create or destroy matter? What percent is destroyed during a chemical reaction? Why sometimes is water: solid ice , liquid liquid water , and gas steam? Is the melting of ice a chemical or physical change? Do bonds break between the hydrogen and oxygen atoms? How can you make particles move faster? In other words, how can you change ice into liquid water? Steel melting is an example of which chemical reaction, phase change or a physical change? Paper burning is an example of which chemical reaction, phase change or a physical change? What is the central part of the atom called the place where protons and neutrons are found? What are positive charge particles in the nucleus called?Link: https://cse.oauife.edu.ng/Exam/70-481.html
- What are neutrally charged particles in the nucleus called? What charge does an electron have? Copy down the picture below and fill in the arrows. Liquid nitrogen and water have low viscosity they flow pretty easily Related documents.Link: https://answers.nuxeo.com/general/q/e4dad12ce9b74ff49ce7341a2f7107be/Error-when-Testing-a-datasource
- Chapter Transition Metals and Coordination Chemistry Ions of the metals, especially the transition metals, are likely to form complexes. Many of these compounds are highly colored Figure 1. In the remainder of this chapter, we will consider the structure and bonding of these remarkable compounds. Figure 1. Metal ions that contain partially filled d subshell usually form colored complex ions; ions with empty d subshell d0 or with filled d subshells d10 usually form colorless complexes. For instance, the four valence electrons of carbon overlap with electrons from four hydrogen atoms to form CH4. The one valence electron leaves sodium and adds to the seven valence electrons of chlorine to form the ionic formula unit NaCl Figure 2.Link: https://answers.microsoft.com/en-us/windows/forum/windows_7-files/openning-userappdatalocaltemp-folder/7f1e931b-ba09-4209-83a5-8e1013821d83
- Transition metals do not normally bond in this fashion. They primarily form coordinate covalent bonds, a form of the Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor Lewis base to an electron acceptor Lewis acid. The Lewis acid in coordination complexes, often called a central metal ion or atom , is often a transition metal or inner transition metal, although main group elements can also form coordination compounds.Link: https://repairclinic.com/Shop-For-Parts/b198/Haier-Parts
- The Lewis base donors, called ligands, can be a wide variety of chemicals—atoms, molecules, or ions. The only requirement is that they have one or more electron pairs, which can be donated to the central metal. Most often, this involves a donor atom with a lone pair of electrons that can form a coordinate bond to the metal. Figure 2. The lone pairs from six water molecules form bonds to the scandium ion to form an octahedral complex. Only the donated pairs are shown. The coordination sphere consists of the central metal ion or atom plus its attached ligands. Brackets in a formula enclose the coordination sphere; species outside the brackets are not part of the coordination sphere.Link: https://chegg.com/homework-help/questions-and-answers/please-show-work-still-confused-even-professors-notes-question-1-observed-persons-suffer-r-q21237883
- The coordination number of the central metal ion or atom is the number of donor atoms bonded to it. In this case, the number of ligands and the coordination number are equal. Figure 3. The geometries of these complexes are the same as we have seen with VSEPR theory for main group elements: linear, tetrahedral, and octahedral. Many other ligands coordinate to the metal in more complex fashions. Bidentate ligands are those in which two atoms coordinate to the metal center. Both of the atoms can coordinate to a single metal center. The most common coordination numbers are two, four, and six, but examples of all coordination numbers from 1 to 15 are known. Figure 4. Many polydentate ligands are chelating ligands, and a complex consisting of one or more of these ligands and a central metal is a chelate. A chelating ligand is also known as a chelating agent. Figure 4 showed one example of a chelate. The heme complex in hemoglobin is another important example Figure 5.Link: https://social.msdn.microsoft.com/Forums/en-US/eb1e7893-f205-4bf7-8403-7301ae68a1a6/searching-for-keywords-code
- It contains a polydentate ligand with four donor atoms that coordinate to iron. Figure 5. The single ligand heme contains four nitrogen atoms that coordinate to iron in hemoglobin to form a chelate. Polydentate ligands are sometimes identified with prefixes that indicate the number of donor atoms in the ligand. Ligands with two donor groups are bidentate ligands. Tridentate ligands, tetradentate ligands, pentadentate ligands, and hexadentate ligands contain three, four, five, and six donor atoms, respectively. The ligand in heme Figure 5 is a tetradentate ligand.Link: https://acloud.guru/course/aws-certified-solutions-architect-associate/discuss/-KC_Wq3Gkq38cpewaFd0/aws-architecture-drawing
- Figure 6. Each of the anionic ligands shown attaches in a bidentate fashion to platinum II , with both a nitrogen and oxygen atom coordinating to the metal. The Naming of Complexes The nomenclature of the complexes is patterned after a system suggested by Alfred Werner, a Swiss chemist and Nobel laureate, whose outstanding work more than years ago laid the foundation for a clearer understanding of these compounds. The following five rules are used for naming complexes: If a coordination compound is ionic, name the cation first and the anion second, in accordance with the usual nomenclature. Name the ligands first, followed by the central metal. Name the ligands alphabetically.Link: https://quora.com/How-selective-is-TU-Delft
- Negative ligands anions have names formed by adding —o to the stem name of the group. For examples, see Table 1. For most neutral ligands, the name of the molecule is used. Anionic Ligand.Link: https://questionpro.com/blog/easy-test-maker/
- We are pretty sure that with the help of these questions, the preparation for exams might become one of the easiest things for the students. That is why they are always looking for the important questions class 11 chemistry chapter 2 for their preparation. This is where Vedantu can be a great help. We have some of the best solutions to the CBSE class 11 chemistry chapter 2 important questions. These questions are selected by our team of experts in order to make sure that students get to have the highest possible marks in the exams. Not to mention that the class 11th chemistry chapter 2 important questions are available for free so that students can download them any time without having to pay a single penny.Link: https://theguardian.com/technology/quiz/2014/aug/07/quiz-internet-slang-bae-how-well-yolo-tbt-mean
- For those who have any mobile devices such as a phone, laptop, or computer, downloading the PDF format of important questions for class 11 chemistry chapter 2 will definitely be easy to do. Our expert teachers have made sure to include the questions that will give the students all the information that they need about the chapter and hence is the most helpful thing ever. Conclusion The class 11 chemistry chapter 2 important questions can be used for the preparation of exams and for revision purposes. However, the students also need to make sure that they are paying attention in their class so that they can get an idea about the chapter, and hence they will be able to answer the questions in the easiest way possible.Link: https://jobnotifys.in/tsspdcl-recruitment-2021/
- The structure of atom class 11 important questions will also help the students in preparing the study routine that they have and they can easily prioritize their time for better results. That is one of the main reasons why Vedantu is considered to be one of the leading names for tutoring sites for students who need just a little bit of help for their class 11 exam preparations.Link: https://law.careers360.com/articles/government-exams-after-llb
- Engage Show students five rods that have the same mass but different volumes. Show students the five rods and explain that they all have the same mass. Then hold up the longest, middle-sized, and shortest rods and remind students that they have the same mass. Ask students to make a prediction: Which rod is the most dense? Least dense? In between? Students may reason that since the mass of each rod is the same, the volume of each rod must have something to do with its density. Some may go so far as to say that the rod with the smallest volume must have the highest density, because the same mass is packed into the smallest volume.Link: http://extrusions.doublehplastics.com/cgi-bin/reading.php?article=cp-biology-final-exam-study-guide-answers-pdf&code=ba042d71e31381848b2b56c34ddf3db3
- Or that the rod with the largest volume must have the lowest density, because the same mass is spread out over the largest volume. Tell students that like the cubes in the previous activity, they will need to know the volume and mass of each of the samples. They will also calculate the density of each sample and use this value to figure out which material each rod is made of. Show an animation and demonstrate how to measure volume using the water displacement method. Project the animation Water Displacement. Play the animation as you demonstrate the water displacement method using a cup of water, a graduated cylinder, and a rod, the way students will do in the activity. Use the dark gray plastic sample so that students can see it better. Volume Demonstrate what students will do by pouring water from a cup into a mL graduated cylinder until it reaches a height that will cover the sample.Link: http://global.oup.com/uk/orc/busecon/business/carmichael/01student/examqs/
- Instead, the surface may curve in a shallow U-shape called the meniscus. When measuring, read the line just at the bottom of the meniscus. Tilt the graduated cylinder and slowly slide the sample into the water. Hold the graduated cylinder upright. Record the level of the water. Subtract the initial water level from the final water level to find the volume of the rod. Students may be confused that the unit for volume in the graduated cylinder is milliliters mL , when in the previous lesson students calculated volume in cubic centimeters cm3. Explain to students that 1 ml is the same as 1 cm3. The volume that the rod takes up pushes or displaces the water. The only place for the water to go is up. The amount or volume of water displaced is equal to the volume of the sample.Link: https://youtube.com/watch?v=MyfweLOInpE
- Is the volume of the sample equal to the final water level? Students should realize that the volume of the rod is not equal to the level of the water in the graduated cylinder. Instead, the volume of the rod equals the amount that the water went up in the graduated cylinder the amount displaced. To find the amount of water displaced, students should subtract the initial level of the water 60 mL from the final level of the water. What units should you use when you record the volume of the sample? Because they will be using the volume to calculate density, students should record the volume of the sample in cm3.Link: http://nebula.wsimg.com/16e14422818312cb9f5bbb0ba9a51a56?AccessKeyId=BCA16D196708CF16A314&disposition=0&alloworigin=1
- Mass Student groups will not need to measure the mass of the rods. The mass of each rod is the same, 15 grams, and is given in their chart on the activity sheet. They will need to measure the volume of each of the five different rods and calculate their densities. Students will use their values for density to identify each rod. Give one activity sheet to each student. Students will record their observations and answer questions about the activity on the activity sheet. The Explain It with Atoms and Molecules and Take It Further sections of the activity sheet will either be completed as a class, in groups, or individually, depending on your instructions.Link: https://fresherslive.com/delhi-public-library-recruitment
Chemistry Chapter 2 Test Answers
Subscribe to:
Post Comments (Atom)
No comments:
Post a Comment