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Lecture 1: Fundamentals of Protein Structure
Lecture 1: Fundamentals of Protein Structure

... -amino (Lys) ...
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... Figure 6a, lanes 5–23). One exception was Gly, which was not incorporated into GFP at all (lanes 4 and 24). Because it was confirmed that Gly was attached to the 3'-end of tRNA like the other amino acids, the complete lack of incorporation was unanticipated. We thus suspected that unknown mechanisms ...
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... Organisms are able to metabolize nutrients other than carbohydrates during times of starvation Once broken down, these monomers are able to feed into various parts of glycolysis or the Krebs cycle (Fig.1, p.117) ...
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REVIEW SHEET FOR RNA AND PROTEIN SYNTHESIS

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... separate parts: a central carbon atom, a carboxyl group (-COOH), an amino group (NH2), a hydrogen, and a „R‟ group. The only difference in the 20 kinds of amino acids is the “R” group. Some “R” groups are very small, others are large, and others form chains and rings. The sequence and shapes of the ...
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Amino Acid Oxidation, the Production of Urea, and Amino Acid

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tacaatccgttat g c cactcatgattagagtcgcgg gatt

... 13._________Genetic code_____________________set of instructions that DNA and RNA use to make proteins 14.________Anticodon____________________the 3 nucleotide sequence in tRNA that is complementary to mRNA. 15._______Translation_________________________process by which mRNA is decoded into a protei ...
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WS 8 – 3: Translation and Protein Synthesis Name

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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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