By G. C. Barrett
This article is meant for undergraduate and starting graduate scholars in chemistry and biochemistry learning amino acids and peptides. The authors be aware of amino acids and peptides with no precise discussions of proteins, whereas giving all of the crucial historical past chemistry, together with series choice, synthesis and spectroscopic equipment. The method is meant to motivate the reader to pass classical limitations whereas gaining an figuring out of protein habit on a molecular point. The publication comprises chapters at the organic roles of amino acids, in addition to a piece on enzyme-catalyzed synthesis of peptides, with appropriate examples, a space usually ignored in texts describing peptide synthesis. this contemporary textual content can be of price within the amino acid, peptide and protein box, to complicated undergraduates, graduate scholars and study staff.
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Extra resources for Amino Acids and Peptides
1987). , 1987). 3 Dipeptides The ﬂexibility of acyclic structures such as peptides has been established convincingly in the broad picture that has emerged from conformational studies. The solution conformation of a dipeptide is sensitive towards (a) the nature of the solvent, (b) the concentration of the solution, (c) the temperature of the solution and (d) the presence and nature of other solutes. The sensitivity is much greater for dipeptides than it is for other acyclic solute molecules, owing to the proximity of the terminal amino and carboxy groups.
G. -glutamic acid and its monosodium salt). Addition of amino acids to the diet is unnecessary for people already eating an adequate and balanced food supply and the toxicity of even the essential amino acids (methionine is the most toxic of all the coded amino acids (Food and Drugs Administration, Washington USA, 1992)) should be better publicised, because some coded amino acids are easily available (for use in specialised diets by ‘body-builders’, for example) and are sometimes used unwisely.
The side-chains are hydrophilic and the overall molecule gains stabilisation through interactions between the side-chains and a polar solvent (such as water); furthermore, amide groups do not easily hydrogen bond with each other. 3 The general case For polypeptides with irregular sequences, as is the usual case for enzymes and other water-soluble globular proteins, the conformational situation ranges from totally random to a mixed situation with regular stretches intermingled with random (irregular) lengths of the backbone.