Amino Acids and Peptides (1998) by G. C. Barrett

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 out precise discussions of proteins, whereas giving the entire crucial historical past chemistry, together with series choice, synthesis and spectroscopic tools. The strategy is meant to motivate the reader to move classical limitations whereas gaining an realizing of protein habit on a molecular point. The e-book contains chapters at the organic roles of amino acids, in addition to a piece on enzyme-catalyzed synthesis of peptides, with compatible examples, a space frequently overlooked in texts describing peptide synthesis. this contemporary textual content might be of price within the amino acid, peptide and protein box, to complicated undergraduates, graduate scholars and study staff.

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R. and Suter, M. (1994) Radiocarbon, 36, 247. Chan, S. J. and Steiner, D. F. (1977) Trends Biochem. , 2, 254. Collingridge, G. L. and Watkins, J. C. (1994) The NMDA Receptor, Second Edition, Oxford University Press, Oxford. Drey, C. N. , in Barrett, G. , Ed. (1985) Chemistry and Biochemistry of the Amino Acids, Chapman & Hall, London, p. 25. Finkelstein, J. D. (1990) J. Nutr. , 1, 228. Food and Drugs Administration, Washington, USA (1992) Safety of Amino Acids used as Dietary Supplements. Hanby, W.

G. g. g. aliphatic hydroxy and side-chain amide groups). The properties of peptides also depend on the same factors, but it must be remembered that, in a linear peptide containing n amino-acid residues, all but one ␣-amino group and one ␣carboxy group are incorporated into neutral peptide and amide bonds. In a cyclic peptide, there are no free ␣-amino or ␣-carboxy groups. Moreover, some peptides contain groups such as carbohydrate, phosphate ester, lipids and porphyrins that further modify physical properties.

The feature of IR spectra for solutions that is useful in the peptide area concerns the hydrogen-bonding property of the amide group. The characteristic carbonyl stretching frequencies of the peptide bond depend on conformation, so IR spectra therefore give some information on conformation. ) can be deliberately designed either to disrupt or to augment hydrogen-bonding interactions and these changes lead to differing stretching frequencies of the amide group. An example of the use of IR to establish the conformational behaviour of a simple dipeptide in solution is shown in Chapter 2.

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