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Amino acids & proteins part 2
Amino acids & proteins part 2

...  After today you should be able to: – Define the structural levels of proteins. – Identify the structural units of the protein backbone. – Explain why some backbone conformations are “forbidden”, i.e. not found in natural proteins. – Name properties on which the amino acids can be grouped. – Name m ...
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... Lipids  are  organic  compounds  that  have  a  large   portion  (much  greater  than  2  to  1)  or  C—H   bonds  and  less  oxygen  than  carbohydrates  (e.g.,   beef  fat  has  the  formula  C57H110O6)   Lipids  are  commonly  call ...
Solutions to 7.012 Problem Set 1
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... strongest type of interaction possible between these amino acids and the cellulose? Cellulose is a polymer of glucose and as such has many free hydroxyl groups. These hydroxyl groups could make hydrogen bonds with any of the charged or uncharged polar amino acids. You may expect serine, threonine, a ...
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Some funcaon of proteins

... substrate  fit  perfectly.  The  enzymes  bind  not  to  the  original   configura9on,  but  to  the  intermediate  state  of  the  substrate  in   their  ac9ve  site  (“induced  fit”)   •  Highly  reac9ve  func9onal  groups  concentrated  in ...
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... into its amino acid subunits. acids legumes grains Isoleucine Then, in the body cells, the X Lysine amino acids are linked in X Valine specific sequences to form X X Histidine new proteins. People can X X Threonine synthesize 11 of the 20 X X Phenylalanine different amino acids by X X Leucine conver ...
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... THE AMINO-ACID-PLP SCHIFF BASE AS SHOWN IN CLASS, SHOW (USING ARROWS TO SHOW FLOW OF ELECTRONS) HOW THE C CARBANION FORMED AFTER CO2 SPLITS OFF IS STABILIZED. ...
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STATE UNIVERSITY OF NEW YORK COLLEGE OF TECHNOLOGY CANTON, NEW YORK
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... Protein synthesis: Adding amino acids & forming peptide bonds Which level of protein structure is being assembled? A. primary B. secondary C. tertiary D. quaternary Microtubules and Microfilaments What do they have in common? A. components of the cytoskeleton B. made of tubulin C. only found in plan ...
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BIOS 1700 Dr. Tanda Week 6, Session 1 1. What two substrates can

... 11. The number of ________ matters regardless of the number of substrates. 12. Enzymes are remarkable biological molecules that catalyze chemical reactions without burning ourselves. The site for chemical reactions in an enzyme is called (A) site and consists of several amino acids. In many cases, t ...
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Lecture Resource ()

... In the PLP-dependent reactions, the bond cleaved in the first step of the reaction depends on the conformation of the amino acid that the enzyme binds ...
Molecole per la vita
Molecole per la vita

... Hydroxy acids, keto acids and amino acids are important polyfunctional compounds: ■■ hydroxy acids contain both the hydroxyl and the carboxyl functional groups; ■■ keto acids are compounds that contain both the carboxyl and the ketone groups; ■■ amino acids contain both the amino and the carboxyl gr ...
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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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