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e. Reference States are critical for the application of empirical
e. Reference States are critical for the application of empirical

... number of parameters. The idea is to use 20 energy parameters to account for the singlebody solvation or hydrophobicity characteristics of each of the different types of amino acids, and a few (2 or 3) additional parameters to account for particular two-body (residue-residue) interactions that are m ...
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... Hydrophobic amino acids contain sulfur. The cysteine is very reactive and involved in the structure of the protein. Involved in disulfide bonds when oxidized. ...
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... carbanion (negative carbon, C-) formed when the first triose GAP (C4-C5-C6) is released. What other mechanisms stabilize carbanions? TPP, the prosthetic group cofactor of decarboxylation enzymes like pyruvate decarboxylase, pyruvate dehydrogenase complex (E1) and a-KG dehydrogenase complex (E1). Bot ...
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... position of DHAP. The general acid catalyst protonating the carbonyl group is His-95. The result is the enediol intermediate. His-95 then functions as a general base abstracting the hydrogen from the hydroxyl group with Glu-165 functioning as a general acid donating its proton to the C2 carbon formi ...
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... move, taste, and see. However, a bag of sugar can remain on the shelf for years without any obvious conversion to CO2 and H2O. Although this chemical process is thermodynamically favorable, it is very slow! Yet when sucrose is consumed by a human (or almost any other organism), it releases its chemi ...
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... 4, values in the right- and left-handed ~ I O / L Y helical regions of the Ramachandran map (4 t60" 2 20", t 30" I20") [ 141. In small peptides, 4+ 1 hydrogen-bonded &turns have been almost exclusively found for Aib-X and X-Aib sequences [11,12]. This residue occurs with considerably lower frequency ...
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Catalytic triad



A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.
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