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A1987K192000001
A1987K192000001

... six-week fast. Furthermore, in prolonged starvation, plasma alanine levels fell to a greater extent than all other amino acids, and the hypoalaninemia, rather than a change in splanchnic fractional extraction of alanine, accounted for the marked reduction in splanchnic alanine uptake observed during ...
Ch. 2 - The Chemistry of Life
Ch. 2 - The Chemistry of Life

...  Include cholesterol, bile salts, vitamin D, and some hormones  Cholesterol is the basis for all steroids made in the body  High levels of cholesterol can lead to heart disease  Excess saturated fats are converted to cholesterol in the body ...
protein synthesis
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... Longer Chain lengths of the fatty acid components Less unsaturation of the fatty acid components Cross linking of fatty acid components ...
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Amino acids and proteins

... When unfolded, all polar/hydrophillic sidechains can interact via Hbonds with water. When the protein folds, they must H-bond to each other and exclude much of the water. All groups capable of forming a hydrogen bond MUST, hence Hbonding in the backbone (C=O to N-H) by way of helices and sheets is a ...
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... • Enzymes are probably the most important type of protein. They act as catalysts to speed up chemical reactions • Enzymes can perform their functions repeatedly, functioning as workhorses that carry out the processes of life ...
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Enzymes: “Helper” Protein molecules

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Biological Molecules

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organic molecules

... VI. Proteins A. Proteins: composed of N, C, H, O B. Polymers called amino acids 1. Amine (NH2) on one end, carboxyl (COOH) on the other end, and H and R groups a. portion that differs: R-group 2. More than 20 different amino acids in nature 3. Sequence of amino acids determines the protein C. 2 ami ...
What amino acids really look like
What amino acids really look like

... Amino acid Structure The central carbon (Cα-atom) is a chiral center Encoded proteins have the L-configuration at this chiral center Configuration can be remembered as the CORN law Looking along the H-Cα bond with H atom closest to you Reading clockwise, the groups attached to the Cα spell CORN ...
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BOTANY DEPARTMENT - university of nairobi staff profiles
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... Purpose The unit aims to provide fundamental concepts with a focus on description, organization, and functions of metabolic pathways of primary metabolites in microorganisms, plants and mammalian systems. Course Objectives 1. To deliver a concise knowledge and understanding of primary basic metaboli ...
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... Alanine (Ala), arginine (Arg), aspartic acid (Asp), cysteine (Cys), glutamic acid (Glu), glycine (Gly), histidine (His), isoleucine (Ile), leucine (Leu), lysine (Lys), methionine (Met), phenylalanine (Phe), proline (Pro), serine (Ser), threonine (Thr), tyrosine (Tyr), valine (Val) VBS0001N, 09/09, u ...
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... The four main classes of organic compounds (carbohydrates, lipids, proteins, and nucleic acids) that are essential to the proper functioning of all living things are known as polymers or macromolecules. All of these compounds are built primarily of carbon, hydrogen, and oxygen but in different ratio ...
Whittier Union High School District
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... 14. What is an enzyme? An enzyme is a type of protein that works like a catalyst. It speeds up reaction by lowering activation energy. 15. What factors can reduce the activity of an enzyme? Temperature, pH level, Ionic conditions or overuse. All of these would make the enzyme not work as efficiently ...
Biomolecule Test Review 2015
Biomolecule Test Review 2015

... 9. What is the difference between saturated and unsaturated fatty acid? Which is better for you? Why? Saturated fatty acid- single bonds, straight and tightly packed. Solid at room temperature. (Bad for us!) Unsaturated fatty acid- double bonds bend the tails and it’s crooked (not straight). Liquid ...
Exam 1
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... A. ____________ The conversion of an alkene into an alcohol is an example of an oxidation reaction. B. ____________The first pKa of NaH2PO4 is about 7. C. ____________ DNA double helices with high G-C content have higher melting points than those with lower G-C content. D. ____________ In blue/white ...
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Review Questions
Review Questions

... The next level is called the tertiary level. Tertiary means “third”. The polypeptide continues to bond to itself but this time the individual amino acids join to each other by bonds between their R groups. Remember, the 20 kinds of amino acids differ because of their R groups. These R groups also h ...
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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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