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CHAPTER 3 ESSENTIALS OF METABOLISM
CHAPTER 3 ESSENTIALS OF METABOLISM

... • In metabolism, respiration occurs at the cellular level and is not the same as breathing (respiration at the macroscopic level). • Cellular respiration describes catabolic processes and is divided into: – Aerobic respiration – metabolism that uses oxygen – Anaerobic respiration– metabolism that do ...
Activated B Complex
Activated B Complex

... vital the B group vitamins are as cofactors for the function of this pathway. If the body is deficient in any of these integral nutrients due to poor supply, reduced absorption or increased demand, it is clear how energy production and well-being may be compromised. Thiamine serves as a cofactor for ...
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Statement of Research Interest - TILT – Colorado State University
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... Using this method we are able to synthesize, -fluoro (halo) substituted -amino acids and -alkoxy substituted -amino acids in good yield and moderate MMP inhibitors. In future I would like to work on this project to improve the designing and drug discovery for MMP inhibitors. Drug discovery for H ...
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Anti-c-myc antibody 9E10 - Protein Engineering, Design and Selection
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... intermediates. GAP and F6P are consumed through glycolysis and oxidative phosphorylation or recycled by gluconeogenesis to form G6P. In the latter case, 1 G6P can be converted, via 6 cycles of pentose phosphate pathway and gluconeogenesis, to 6 CO2 and 12 NADPH. • When R5P is needed more than NADPH, ...
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... • That’s where Transfer RNA or tRNA comes in. As the ribosome reads the nucleotide triplet (codon) of mRNA, a specific tRNA molecule matches up with the sequence and carries with it a specific amino acid. • The amino acid then binds to the growing amino acid (polypeptide) chain until the mRNA messag ...
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... and 384, while ]3a has the different residues to those, as shown in the comparison table. The substitution of threonine for alanine at position 339 may not be responsible for the serological difference, because both residues appear in all subclasses. Accordingly, the presence of serine residue at po ...
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Chapter 13.1 and 13.2 RNA, Ribosomes, and Protein Synthesis
Chapter 13.1 and 13.2 RNA, Ribosomes, and Protein Synthesis

... cytoplasm. – On ribosome, translation begins at START codon. – Each codon attracts an anticodon aka tRNA – tRNA carries an amino acid. – Amino acids bond and move along the mRNA – Continues until reaches STOP codon and forms polypeptide and mRNA is released. ...
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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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