Amino Acids and Peptides 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 pay attention to amino acids and peptides with no specific discussions of proteins, whereas giving all of the crucial historical past chemistry, together with series selection, synthesis and spectroscopic tools. The method is meant to inspire the reader to move classical barriers whereas gaining an figuring out 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 appropriate examples, a space frequently ignored in texts describing peptide synthesis. this contemporary textual content should be of price within the amino acid, peptide and protein box, to complicated undergraduates, graduate scholars and study employees.

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Hermkens, P. H. , van Dinther, T. , Joukema, C. , Wagenaars, G. N. and Ottenheijm, H. C. , 35, 9271. , Buttkus, U. -H. (1991) Angew. Chem. Int. , 30, 1514. Zimm, B. , and Bragg, J. K. (1959) J. Chem. , 31, 526. 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.

1 Amino acids in chemistry The physiological importance of ␣-amino acids ensures a sustained interest in their chemistry – particularly in pharmaceutical exploration for new drugs, and for their synthesis, reactions and physical properties. As is often the case when the chemistry of a biologically important class of compounds is being vigorously developed, an increasing range of uses has been identified for ␣-amino acids in the wider context of stereoselective laboratory synthesis (including studies of biomimetic synthetic routes).

5 General aspects of ultraviolet (UV) spectrometry, circular dichroism (CD) and UV fluorescence spectrometry These techniques are intimately related, since their spectral features originate in the same physical event, namely the absorption within locations (chromophores) of the amino acid or peptide of light from the ultraviolet wavelength region (␭ ϭ200–400 nm) and from longer (visible) wavelengths for coloured compounds. The chromophores that respond to electronic excitation which are common to amino acids and peptides are the amino, carboxy and amide groups.

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