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Understanding Acid Lability of Cysteine Protecting Groups
Understanding Acid Lability of Cysteine Protecting Groups

document/47414 - UvA-DARE
document/47414 - UvA-DARE

... enzymes to simple organic acid intermediates that enter general metabolism (figure 1). The catabolic pathways of the BCAAs can be divided into two sequential series of reactions, referred to as the common pathway and the distal pathway. The process begins with the transport of the BCAAs via a Na+-de ...
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Peptide Chemistry and Drug Design Brochure

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Answers to Scoring in Scrabble (English Word Play)
Answers to Scoring in Scrabble (English Word Play)

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ENZYME STUDIES ON CHROMOSOMES [ 40 ]
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... The inactivity of the intracellular proteases raises interesting questions. Certainly these split many bonds in a solution of a protein like albumin. Is there some physical condition which prevents their attack on the same bonds in a fiber? Or are these bonds so placed in the fiber that the fiber co ...
Liver - KSU Faculty Member websites
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Chapter 12: Protein structure, stability and folding
Chapter 12: Protein structure, stability and folding

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Disruption of Glucocorticoid and Mineralocorticoid Receptor
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... none of the identified compounds was of high potency. It cannot be excluded at this point that some of the identified chemicals have more pronounced effects under certain conditions such as oxidative stress or upon preincubation for a prolonged time. Clearly, a more extensive screening will be neces ...
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... survived a malathion screen carried the allele for glycine, while those wasps that died did not have the allele for glycine. At position 1122 (Fig. 1), an adenine in the susceptible strain is substituted by a guanine in the resistant strain. This nucleotide difference does not lead to a change in th ...
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Comparing Kernels For Predicting Protein Binding Sites From Amino
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... problems in functional genomics. Protein-protein, proteinDNA, and protein-RNA interactions play a pivotal role in protein functions. Experimental detection of residues in protein-protein interaction surfaces must come from determination of the structure of protein-protein, protein-DNA and protein-RN ...
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Two fatty acid ∆9-desaturase genes, ole1 and ole2
Two fatty acid ∆9-desaturase genes, ole1 and ole2

... Genes encoding two distinct fatty acid ∆9-desaturases were isolated from strains of the oleaginous fungus Mortierella alpina. Two genomic sequences, ∆9-1 and ∆9-2, each containing a single intron, were cloned from strain CBS 528.72 while one cDNA clone, LM9, was isolated from strain CBS 210.32. The ...
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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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