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Table Of Contents

2.2Configurational isomerism within the peptide bond
2.3 Dipeptides
2.4 Cyclic oligopeptides
2.5Acyclic oligopeptides
2.6Longer oligopeptides:primary,secondary and tertiary structure
2.7Polypeptides and proteins:quaternary structure and aggregation
2.8.1The main categories ofpolypeptide conformation
2.8.1.1One extreme situation
2.8.1.2The other extreme situation
2.8.1.3The general case
2.10 References
Physicochemical properties of amino acids and peptides
3.1 Acid–base properties
3.2Metal-binding properties ofamino acids and peptides
3.4Infrared (IR) spectrometry
3.6 Circular dichroism
3.7Nuclear magnetic resonance (NMR) spectroscopy
3.9 References
Reactions and analytical methods for amino acids and peptides
Part 1.Reactions ofamino acids and peptides
4.1Introduction
4.2General survey
4.2.1Pyrolysis ofamino acids and peptides
4.2.2Reactions ofthe amino group
4.2.3Reactions ofthe carboxy group
4.2.4Reactions involving both amino and carboxy groups
4.3A more detailed survey ofreactions ofthe amino group
4.3.1N-Acylation
4.3.2Reactions with aldehydes
4.3.3N-Alkylation
4.4A survey ofreactions ofthe carboxy group
4.4.2 Oxidative decarboxylation
4.5Derivatisation ofamino acids for analysis
4.7.1Mass spectra offree amino acids
4.7.2Mass spectra offree peptides
4.7.3Negative-ion mass spectrometry
4.8Examples ofmass spectra ofpeptides
4.8.2Finer details ofmass spectra ofpeptides
4.8.3Difficulties and ambiguities
4.10 Early methodology: peptide derivatisation
4.10.1 N-Terminal acylation and C-terminal esterification
4.10.2N-Acylation and N-alkylation ofthe peptide bond
4.10.3Reduction ofpeptides to ‘polyamino-polyalcohols’
4.11.1 Current methodology: instrumental variations
4.16Molecular exclusion chromatography (gel chromatography)
4.17Electrophoretic separation and ion-exchange chromatography
4.17.1Capillary zone electrophoresis (CZE)
4.18Detection ofseparated amino acids and peptides
4.18.2Detection ofamino acids and peptides separated by GLC
4.19Thin-layer chromatography (planar chromatography;HPTLC)
4.20Quantitative amino-acid analysis
4.21References
Part 4.Immunoassays for peptides
4.22 Radioimmunoassays
4.23Enzyme-linked immunosorbent assays (ELISAs)
4.24References
Part 5.Enzyme-based methods for amino acids
4.25Biosensors
4.26References
Determination of the primary structures of peptides and proteins
5.3Cleavage ofdisulphide bonds
5.4Identification ofthe N-terminus and stepwise degradation
5.5Enzymic methods for determining N-terminal sequences
5.6 Identification of C-terminal sequences
5.7Enzymic determination of C-terminal sequences
5.8Selective chemical methods for cleaving peptide bonds
5.9Selective enzymic methods for cleaving peptide bonds
5.10Determination ofthe positions ofdisulphide bonds
5.12Determination ofthe sequence ofDNA
5.13 References
Synthesis of amino acids
6.1General
6.2Commercial and research uses for amino acids
6.3Biosynthesis:isolation ofamino acids from natural sources
6.3.1Isolation ofamino acids from proteins
6.6Other general methods ofamino-acid synthesis
6.7Resolution ofDL-amino acids
6.8Asymmetric synthesis ofamino acids
6.9 References
Methods for the synthesis of peptides
7.1Basic principles ofpeptide synthesis and strategy
7.4 Protection of carboxy groups
7.5 Protection of functional side-chains
7.5.1Protection of -amino groups
7.5.2Protection ofthiol groups
7.5.3Protection ofhydroxy groups
7.5.4Protection ofthe guanidino group ofarginine
7.5.5Protection ofthe imidazole ring ofhistidine
7.5.6Protection ofamide groups
7.5.7Protection ofthe thioether side-chain ofmethionine
7.5.8Protection ofthe indole ring oftryptophan
7.6 Deprotection procedures
7.8Methods for forming peptide bonds
7.8.1The acyl azide method
7.8.2The use ofacid chlorides and acid fluorides
7.8.3The use ofacid anhydrides
7.8.4The use ofcarbodiimides
7.8.5The use ofreactive esters
7.8.6The use ofphosphonium and isouronium derivatives
7.9Solid-phase peptide synthesis (SPPS)
7.10 Soluble-handle techniques
7.11Enzyme-catalysed peptide synthesis and partial synthesis
7.12Cyclic peptides
7.12.1Homodetic cyclic peptides
7.12.2Heterodetic cyclic peptides
7.13The formation ofdisulphide bonds
7.14 References
7.14.1References cited in the text
7.14.2References for background reading
Biological roles of amino acids and peptides
8.2The role ofamino acids in protein biosynthesis
8.3Post-translational modification ofprotein structures
8.4Conjugation ofamino acids with other compounds
8.5Other examples ofsynthetic uses ofamino acids
8.6Important products ofamino-acid metabolism
8.8 The biosynthesis of penicillins and cephalosporins
8.9 References
8.9.1References cited in the text
8.9.2References for background reading
Some aspects of amino-acid and peptide drug design
9.1 Amino-acid antimetabolites
9.2Fundamental aspects ofpeptide drug design
9.3The need for peptide-based drugs
9.4The mechanism ofaction ofproteinases and design ofinhibitors
9.5Some biologically active analogues ofpeptide hormones
9.6The production ofantibodies and vaccines
9.7The combinatorial synthesis ofpeptides
9.8The design ofpro-drugs based on peptides
9.9 Peptide antibiotics
9.10 References
9.10.1References cited in the text
9.10.2References for background reading
Subject index
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acids and Peptides

acids and Peptides

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Published by Tarekegn Gebreyesus

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Published by: Tarekegn Gebreyesus on Dec 14, 2010
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11/09/2011

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