Cover -- Half-title -- Title -- Copyright -- Contents -- Foreword -- Supplementary reading (see also lists at the end of each Chapter) -- Standard Student Texts -- Supplementary reading: suggestions for further reading -- (a) Protein structure -- (b) Protein chemistry -- (c) Amino acids -- (d) Peptides -- 1 Introduction -- 1.1 Sources and roles of amino acids and peptides -- 1.2 Definitions -- 1.3 'Protein amino acids', alias 'the coded amino acids' -- 1.4 Nomenclature for 'the protein amino acids', alias 'the coded amino acids' -- 1.5 Abbreviations for names of amino acids and the use of these abbreviations to give names to polypeptides -- 1.6 Post-translational processing: modifications of amino-acid residues within polypeptides -- 1.7 Post-translational processing: in vivo cleavages of the amide backbone of polypeptides -- 1.8 'Non-protein amino acids', alias 'non-proteinogenic amino acids' or 'non-coded amino acids' -- 1.9 Coded amino acids, non-natural amino acids and peptides in nutrition and food science and in human physiology -- 1.10 The geological and extra-terrestrial distribution of amino acids -- 1.11 Amino acids in archaeology and in forensic science -- 1.12 Roles for amino acids in chemistry and in the life sciences -- 1.12.1 Amino acids in chemistry -- 1.12.2 Amino acids in the life sciences -- 1.13 Beta- and higher amino acids -- 1.14 References -- 2 Conformations of amino acids and peptides -- 2.1 Introduction: the main conformational features of amino acids and peptides -- 2.2 Configurational isomerism within the peptide bond -- 2.3 Dipeptides -- 2.4 Cyclic oligopeptides -- 2.5 Acyclic oligopeptides -- 2.6 Longer oligopeptides: primary, secondary and tertiary structure -- 2.7 Polypeptides and proteins: quaternary structure and aggregation -- 2.8 Examples of conformational behaviour.

ordered and disordered states and transitions between them -- 2.8.1 The main categories of polypeptide conformation -- 2.8.1.1 One extreme situation -- 2.8.1.2 The other extreme situation -- 2.8.1.3 The general case -- 2.9 Conformational transitions for peptides -- 2.10 References -- 3 Physicochemical properties of amino acids and peptides -- 3.1 Acid-base properties -- 3.2 Metal-binding properties of amino acids and peptides -- 3.3 An introduction to the routine aspects and the specialised aspects of the spectra of amino acids and peptides -- 3.4 Infrared (IR) spectrometry -- 3.5 General aspects of ultraviolet (UV) spectrometry, circular dichroism (CD) and UV fluorescence spectrometry -- 3.6 Circular dichroism -- 3.7 Nuclear magnetic resonance (NMR) spectroscopy -- 3.8 Examples of assignments of structures to peptides from NMR spectra and other data -- 3.9 References -- 4 Reactions and analytical methods for amino acids and peptides -- Part 1. Reactions of amino acids and peptides -- 4.1 Introduction -- 4.2 General survey -- 4.2.1 Pyrolysis of amino acids and peptides -- 4.2.2 Reactions of the amino group -- 4.2.3 Reactions of the carboxy group -- 4.2.4 Reactions involving both amino and carboxy groups -- 4.3 A more detailed survey of reactions of the amino group -- 4.3.1 N-Acylation -- 4.3.2 Reactions with aldehydes -- 4.3.3 N-Alkylation -- 4.4 A survey of reactions of the carboxy group -- 4.4.1 Esterification -- 4.4.2 Oxidative decarboxylation -- 4.4.3 Reduction -- 4.4.4 Halogenation -- 4.4.5 Reactions involving amino and carboxy groups of Alpha-amino acids and their N-acyl derivatives -- 4.4.6 Reactions at the Alpha-carbon atom and racemisation of Alpha-amino acids -- 4.4.7 Reactions of the amide group in acylamino acids and peptides -- 4.5 Derivatisation of amino acids for analysis.

4.5.1 Preparation of N-acylamino acid esters and similar derivatives for analysis -- 4.6 References -- Part 2. Mass spectrometry in amino-acid and peptide analysis and in peptide sequence determination -- 4.7 General considerations -- 4.7.1 Mass spectra of free amino acids -- 4.7.2 Mass spectra of free peptides -- 4.7.3 Negative-ion mass spectrometry -- 4.8 Examples of mass spectra of peptides -- 4.8.1 Electron-impact mass spectra (EIMS) of peptide derivatives -- 4.8.2 Finer details of mass spectra of peptides -- 4.8.3 Difficulties and ambiguities -- 4.9 The general status of mass spectrometry in peptide analysis -- 4.9.1 Specific advantages of mass spectrometry in peptide sequencing -- 4.10 Early methodology: peptide derivatisation -- 4.10.1 N-Terminal acylation and C-terminal esterification -- 4.10.2 N-Acylation and N-alkylation of the peptide bond -- 4.10.3 Reduction of peptides to 'polyamino-polyalcohols' -- 4.11 Current methodology: sequencing by partial acid hydrolysis, followed by direct MS analysis of peptide hydrolysates -- 4.11.1 Current methodology: instrumental variations -- 4.12 Conclusions -- 4.13 References -- Part 3. Chromatographic and related methods for the separation of mixtures of amino acids, mixtures of peptides and mixtures… -- 4.14 Separation of amino-acid and peptide mixtures -- 4.14.1 Separation principles -- 4.15 Partition chromatography -- HPLC and GLC -- 4.16 Molecular exclusion chromatography (gel chromatography) -- 4.17 Electrophoretic separation and ion-exchange chromatography -- 4.17.1 Capillary zone electrophoresis (CZE) -- 4.18 Detection of separated amino acids and peptides -- 4.18.1 Detection of amino acids and peptides separated by HPLC and by other liquid-based techniques -- 4.18.2 Detection of amino acids and peptides separated by GLC -- 4.19 Thin-layer chromatography (planar chromatography -- HPTLC).

4.20 Quantitative amino-acid analysis -- 4.21 References -- Part 4. Immunoassays for peptides -- 4.22 Radioimmunoassays -- 4.23 Enzyme-linked immunosorbent assays (ELISAs) -- 4.24 References -- Part 5. Enzyme-based methods for amino acids -- 4.25 Biosensors -- 4.26 References -- 5 Determination of the primary structures of peptides and proteins -- 5.1 Introduction -- 5.2 Strategy -- 5.3 Cleavage of disulphide bonds -- 5.4 Identification of the N-terminus and stepwise degradation -- 5.5 Enzymic methods for determining N-terminal sequences -- 5.6 Identification of C-terminal sequences -- 5.7 Enzymic determination of C-terminal sequences -- 5.8 Selective chemical methods for cleaving peptide bonds -- 5.9 Selective enzymic methods for cleaving peptide bonds -- 5.10 Determination of the positions of disulphide bonds -- 5.11 Location of post-translational modifications and prosthetic groups -- 5.12 Determination of the sequence of DNA -- 5.13 References -- 6 Synthesis of amino acids -- 6.1 General -- 6.2 Commercial and research uses for amino acids -- 6.3 Biosynthesis: isolation of amino acids from natural sources -- 6.3.1 Isolation of amino acids from proteins -- 6.3.2 Biotechnological and industrial synthesis of coded amino acids -- 6.4 Synthesis of amino acids starting from coded amino acids other than glycine -- 6.5 General methods of synthesis of amino acids starting with a glycine derivative -- 6.6 Other general methods of amino-acid synthesis -- 6.7 Resolution of DL-amino acids -- 6.8 Asymmetric synthesis of amino acids -- 6.9 References -- 7 Methods for the synthesis of peptides -- 7.1 Basic principles of peptide synthesis and strategy -- 7.2 Chemical synthesis and genetic engineering -- 7.3 Protection of Alpha-amino groups -- 7.4 Protection of carboxy groups -- 7.5 Protection of functional side-chains -- 7.5.1 Protection of Epsilon-amino groups.

7.5.2 Protection of thiol groups -- 7.5.3 Protection of hydroxy groups -- 7.5.4 Protection of the guanidino group of arginine -- 7.5.5 Protection of the imidazole ring of histidine -- 7.5.6 Protection of amide groups -- 7.5.7 Protection of the thioether side-chain of methionine -- 7.5.8 Protection of the indole ring of tryptophan -- 7.6 Deprotection procedures -- 7.7 Enantiomerisation during peptide synthesis -- 7.8 Methods for forming peptide bonds -- 7.8.1 The acyl azide method -- 7.8.2 The use of acid chlorides and acid fluorides -- 7.8.3 The use of acid anhydrides -- 7.8.4 The use of carbodiimides -- 7.8.5 The use of reactive esters -- 7.8.6 The use of phosphonium and isouronium derivatives -- 7.9 Solid-phase peptide synthesis (SPPS) -- 7.10 Soluble-handle techniques -- 7.11 Enzyme-catalysed peptide synthesis and partial synthesis -- 7.12 Cyclic peptides -- 7.12.1 Homodetic cyclic peptides -- 7.12.2 Heterodetic cyclic peptides -- 7.13 The formation of disulphide bonds -- 7.14 References -- 7.14.1 References cited in the text -- 7.14.2 References for background reading -- 8 Biological roles of amino acids and peptides -- 8.1 Introduction -- 8.2 The role of amino acids in protein biosynthesis -- 8.3 Post-translational modification of protein structures -- 8.4 Conjugation of amino acids with other compounds -- 8.5 Other examples of synthetic uses of amino acids -- 8.6 Important products of amino-acid metabolism -- 8.7 Glutathione -- 8.8 The biosynthesis of penicillins and cephalosporins -- 8.9 References -- 8.9.1 References cited in the text -- 8.9.2 References for background reading -- 9 Some aspects of amino-acid and peptide drug design -- 9.1 Amino-acid antimetabolites -- 9.2 Fundamental aspects of peptide drug design -- 9.3 The need for peptide-based drugs -- 9.4 The mechanism of action of proteinases and design of inhibitors.

9.5 Some biologically active analogues of peptide hormones.