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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 out unique discussions of proteins, whereas giving all of the crucial heritage chemistry, together with series choice, synthesis and spectroscopic equipment. The strategy is meant to inspire the reader to pass classical limitations whereas gaining an knowing of protein habit on a molecular point. The ebook comprises chapters at the organic roles of amino acids, in addition to a bit on enzyme-catalyzed synthesis of peptides, with compatible examples, a space usually 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 learn staff.

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3. Representative peptides made up from -␣-amino acids. (a) The structural formula of a parallel ␤-sheet showing H-bonds. (b) The structural formula of a righthanded ␣-helix showing H-bonds. (c) The standard ‘tape’ depictions of the right-handed ␣-helix and antiparallel ␤-sheet. All amide bonds are in the trans configuration. numerous physical phenomena (gel formation as gelatin solutions are cooled, which is mimicked by the behaviour of some synthetic oligopeptide solutions) and more subtle aspects of protein behaviour of physiological importance.

The industrial production base that has been developed to meet these demands (see Chapter 6) makes many amino acids cheaply available for other purposes such as laboratory use and has contributed in no small measure to the development of the biotechnological sector of the chemical industry. 10 The geological and extra-terrestrial distribution of amino acids The development of sensitive analytical methods for amino acids became an essential support for the study of geological specimens (terrestrial ones and Lunar and Martian samples) from the 1970s.

This is because of the wider distribution and greater ease of use of X-ray crystallography equipment nowadays. The conformational behaviour of N- and C-terminal-derivatised amino acids and peptides in organic solvents has also been studied, particularly by nuclear magnetic resonance and circular dichroism spectrometric techniques (in which advances in instrumentation have been very considerable; see Chapter 3). 2 Configurational isomerism within the peptide bond The amide group shows restricted flexibility because its central —NH—CO— bond has some double-bond character due to resonance stabilisation [—NH—CO— ↔—NϩH෇C(OϪ)—].

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