Read e-book online Amino Acids and Peptides (1998) PDF

By G. C. Barrett

ISBN-10: 0511039522

ISBN-13: 9780511039522

ISBN-10: 0521462924

ISBN-13: 9780521462921

ISBN-10: 0521468272

ISBN-13: 9780521468275

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 out designated discussions of proteins, whereas giving all of the crucial heritage chemistry, together with series decision, synthesis and spectroscopic tools. The process is meant to motivate the reader to pass classical limitations 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 bit on enzyme-catalyzed synthesis of peptides, with compatible examples, a space frequently overlooked in texts describing peptide synthesis. this contemporary textual content can be of worth within the amino acid, peptide and protein box, to complicated undergraduates, graduate scholars and examine staff.

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Extra info for Amino Acids and Peptides (1998)

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B) A ␥-turn. 4). 4). 1(b)) for the backbone single bonds (␻ for the C(O)—N bond, ␾ for the C␣—N bond, ␺ for the C␣—C bond) and ␹1 for the C␣—side-chain-C␤—bond, ␹2 for the C␤—C␥ bond, etc. 2). Trans- and cis peptide bonds have ␻ ϭ180º and this is the torsion angle seen in all flexible peptides constructed from ␣-amino acids. For poly(-alanine), in its usual right-handed ␣-helix, ␺ is Ϫ47º and ␾ is Ϫ57º. There are several types of ␣-helix and of ␤-bends, all differing slightly in torsion angles within the residues of the actual turn and, in the case of the ␣-helix, also determined by the pattern of intramolecular and intermolecular hydrogen bonding.

A representative dipeptide made up from -␣-amino acids, in the extended conformation with the amide bond in the trans configuration. amino acids, assist the adoption of more flexible structures by peptides when they are built into peptides, because mixtures of cis and trans configurations are more likely. Cis-amide bonds are rare in natural polypeptides that contain no proline residues (there are three cis-amide bonds in the enzyme carboxypeptidase A and one in the smaller polypeptide concanavalin A), though current re-investigations by NMR methods (Chapter 3) are revealing more distorted trans-amide bonds in structures established without such details in the early days of X-ray crystallography.

E. the Bouguer–Beer–Lambert law does not apply to CD spectra). e. the UV spectrum), which has no sign. The CD spectrum can be interpreted in terms of absolute configuration; the sign of a particular CD feature corresponds to a particular absolute configuration of the solute, for the chiral centre nearest the chromophore responsible for that CD feature. Information on conformation (based on the sign and specific details of an overall CD spectrum for a compound of known absolute configuration) can be obtained for amino acids and peptides.

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


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