Note: AMINO ACIDS, PEPTIDES AND PROTEINS -- Contents -- Chapter 1 Amino Acids -- 1 Introduction -- 2 Textbooks and Reviews -- 3 Naturally Occurring Amino Acids -- 3.1 Isolation of Amino Acids from Natural Sources -- 3.2 Occurrence of Known Amino Acids -- 3.3 New Naturally Occurring Amino Acids -- 3.4 New Amino Acids from Hydrolysates -- 4 Chemical Synthesis and Resolution of Amino Acids -- 4.1 General Methods for the Synthesis of α-Amino Acids -- 4.2 Asymmetric Synthesis of α-Amino Acids -- 4.3 Synthesis of Protein Amino Acids and Other Naturally Occurring α-Amino Acids -- 4.4 Synthesis of α-Amino Analogues of Protein Amino Acids and Other Natural α-Amino Acids -- 4.5 Synthesis of α-Amino Acids Carrying Alkyl Side-chains, and Cyclic Analogues -- 4.6 Models for Prebiotic Synthesis of Amino Acids -- 4.7 Synthesis of α-Alkoxy α-Amino Acids, and Analogous α-Hetero-atom Substituted α-Amino Acids -- 4.8 Synthesis of α-(ω-Halogenoalkyl)-α-Amino Acids -- 4.9 Synthesis of α-(ω-Hydroxyalkyl)-α-Amino Acids -- 4.10 Synthesis of N-Substituted α-Amino Acids -- 4.11 Synthesis of α-Amino Acids Carrying Unsaturated Aliphatic Side-chains -- 4.12 Synthesis of α-Amino Acids with Aromatic or Heteroaromatic Side-chains -- 4.13 Synthesis of α-(N-Hydroxyamino) Acids -- 4.14 Synthesis of α-Amino Acids Carrying Aminoalkyl Groups, and Related Nitrogen Functional Groups, in Side-chains -- 4.15 Synthesis of α-Amino Acids Carrying Sulfur-, Selenium- or Tellurium-containing Side-chains -- 4.16 Synthesis of α-Amino Acids Carrying Phosphorus Functional Groups in Side-chains -- 4.17 Synthesis of α-Amino Acids Carrying Boron Functional Groups in Side-chains -- 4.18 Synthesis of Isotopically Labelled α-Amino Acids -- 4.19 Synthesis of β-Amino Acids and Higher Homologous Amino Acids -- 4.20 Resolution of DL-Amino Acids -- 5 Physico-chemical Studies of Amino Acids. , 5.1 X-Ray Crystal Analysis of Amino Acids and Their Derivatives -- 5.2 Nuclear Magnetic Resonance Spectrometry -- 5.3 Optical Rotatory Dispersion and Circular Dichroism -- 5.4 Mass Spectrometry -- 5.5 Other Spectroscopic Studies of Amino Acids -- 5.6 Physico-chemical Studies of Amino Acids -- 5.7 Molecular Orbital Calculations for Amino Acids -- 6 Chemical Studies of Amino Acids -- 6.1 Racemization -- 6.2 General Reactions of Amino Acids -- 6.2.1 Reactions at the Amino Group -- 6.2.2 Reactions at the Carboxy Group -- 6.2.3 Reactions Involving Both Amino and Carboxy Groups -- 6.2.4 Reactions at the α-Carbon Atom of α-Amino Acids -- 6.2.5 Reactions Specific to β- and Higher Homologous Amino Acids -- 6.3 Specific Reactions of Amino Acids -- 6.4 Effects of Electromagnetic Radiation on Amino Acids -- 7 Analytical Methods -- 7.1 Introduction -- 7.2 Gas-Liquid Chromatography -- 7.3 Ion-exchange Chromatography -- 7.4 Thin-layer Chromatography -- 7.5 High-performance Liquid Chromatography -- 7.6 Fluorimetric Analysis -- 7.7 Capillary Zone Electrophoresis and Other Analytical Methods -- 7.8 Assays for Specific Amino Acids -- References -- Chapter 2 Peptide Synthesis -- 1 Introduction -- 2 Methods -- 2.1 Amino-group Protection -- 2.2 Carboxyl-group Protection -- 2.3 Side-chain Protection -- 2.4 Disulfide Bond Formation -- 2.5 Peptide Bond Formation -- 2.6 Peptide Synthesis on Macromolecular Support and Methods of Combinatorial Synthesis -- 2.7 Enzyme-mediated Synthesis and Semisynthesis -- 2.8 Miscellaneous Reactions Related to Peptide Synthesis -- 3 Appendix: A List of Syntheses Reported Mainly in 1996 -- 3.1 Natural Peptides, Proteins and Partial Sequences -- 3.2 Sequential Oligo- and Poly-peptides -- 3.3 Enzyme Substrates and Inhibitors -- 3.4 Conformation of Synthetic Peptides -- 3.5 Glycopeptides -- 3.6 Phosphopeptides and Related Compounds. , 3.7 Immunogenic Peptides -- 3.8 Nucleopeptides, PNAs -- 3.9 Miscellaneous Peptides -- 3.10 Purification Methods -- References -- Chapter 3 Analogue and Conformational Studies on Peptides, Hormones and Other Biologically Active Peptides -- 1 Introduction -- 2 Peptide Backbone Modifications and Di-, Tri-Peptide Mimetics -- 2.1 ψ[CH2NH]-Aminomethylene, ψ[CH(CN)NH]- Cyanomethyleneamino and ψ[CH2O]-Ether Analogues -- 2.2 ψ[CH=CH]-Isosteres and Related Analogues -- 2.3 ψ[COCH2]-Ketomethylene, α-Hydroxy Ketomethylene and Ketovinyl Isosteres -- 2.4 Retro and Retro-inverso Pseudo Peptides -- 2.5 Azapeptides -- 2.6 Rigid Di-, Tri-peptide and Turn Mimetics -- 3 Cyclic Peptides -- 3.1 Conformational Studies -- 3.2 Naturally Occurring Cyclic Peptides -- 4 Biologically Active Peptides -- 4.1 Peptides Involved in Alzheimer's Disease -- 4.2 Antimicrobial Peptides -- 4.3 ACTH/CRF Peptides -- 4.4 Angiotensin II Analogues and Non-peptide Angiotensin II Receptor Ligands -- 4.5 Bombesin/Neuromedin Analogues -- 4.6 Bradykinin Analogues -- 4.7 Cholecystokinin Analogues -- 4.8 Endothelin Analogues -- 4.9 Growth Hormone-releasing Peptide and Non-peptide Analogues -- 4.10 Integrin Related Peptide and Non-peptide Analogues -- 4.11 LHRH Analogues -- 4.12 Neuropeptide Y (NPY) Analogues -- 4.13 Opioid (Enkephalin, β-Casomorphin, Morphiceptin, Deltorphin and Dynorphin) Peptides -- 4.14 Somatostatin Analogues -- 4.15 Tachykinin (Substance P and Neurokinins) Analogues -- 4.16 Thrombin Receptor Peptides -- 4.17 Thyrotropin-releasing Hormone Analogues -- 4.18 Vasopressin and Oxytocin Analogues -- 5 Enzyme Inhibitors -- 5.1 Converting Enzymes [Angiotensin (ACE), Neutral Endopeptidase (NEP), Endothelin and Interleukin-1 β (ICE) Inhibitors -- 5.1.1 Angiotensin Converting Enzyme and Neutral Endopeptidase Inhibitors -- 5.1.2 Endothelin Converting Enzyme Inhibitors. , 5.1.3 Interleukin-1 β Converting Enzyme Inhibitors -- 5.2 Ras Protein Farnesyltransferase Inhibitors -- 5.3 HIV Protease Inhibitors -- 5.4 Matrix Metalloproteinase Inhibitors -- 5.5 Inhibitors of Renin (Aspartyl Protease) -- 5.6 Inhibitors of Thrombin (Serine Protease) -- 5.7 Miscellaneous (Calpain, Cathepsin B, Cathepsin D, Elastase, Protein-tyrosine Kinase, Protein-tyrosine Phosphatase and Virus Ribonucleotide Reductase) Inhibitors -- 6 Advances in Formulation/Delivery Technology -- References -- Chapter 4 Cyclic, Modified and Conjugated Peptides -- 1 Introduction -- 2 Cyclic Peptides -- 2.1 General Considerations -- 2.2 Dioxopiperazines (Cyclic Dipeptides) -- 2.3 Cyclotripeptides -- 2.4 Cyclotetrapeptides -- 2.5 Cyclopentapeptides -- 2.6 Cyclohexapeptides -- 2.7 Cycloheptapeptides -- 2.8 Cyclooctapeptides -- 2.9 Cyclononapeptides and Cyclodecapeptides -- 2.10 Hugher Cyclic Peptides -- 2.11 Peptides Containing Thiazole/Oxazole Rings -- 2.12 Cyclodepsipeptides -- 3 Modified and Conjugated Peptides -- 3.1 Phosphopeptides -- 3.2 Glycopeptide Antibiotics -- 3.3 Glycopeptides -- 3.4 Lipopeptides -- 3.5 Miscellaneous Conjugates -- 4 Miscellaneous Structures -- References -- Chapter 5 Metal Complexes of Amino Acids and Peptides -- 1 Introduction -- 2 Amino Acid Complexes -- 2.1 Synthesis and Structural Studies -- 2.2 Solution Studies -- 2.3 Kinetic Studies -- 3 Peptide Complexes -- 3.1 Synthesis and Structures of Peptide Complexes -- 3.2 Reactivity - Metal-ion-assisted Transformations of Peptide Molecules -- 3.3 Solution Equilibria - Stability Constants of Metal-ion-Peptide Complexes -- References -- Chapter 6 Current Trends in Protein Research -- 1 Introduction -- 2 Protein Folding -- 2.1 New Methods -- 2.2 Chaperones and Protein Folding -- 3 Techniques - Mass Spectrometry -- 4 Extremophilic Proteins -- 4.1 Antifreeze Proteins. , 4.2 Thermophilic Proteins -- 4.2.1 Elongation Factor Ts (EF-TS) from Thermus thermophilus -- 4.2.2 DNA Polymerase/DNA Complex Thermus aquaticus -- 4.2.3 Ribosomal Protein L1 (Thermus thermophilus) -- 4.2.4 Ribosomal Protein L14 (Bacillus stearothermophilus) -- 4.2.5 Ribosomal Protein S8 (Bacillus stearothermophilus) -- 4.2.6 D-Glyceraldehyde-3-phosphate dehydrogenase (Thermus aquaticus) -- 4.2.7 Methanothermus fervidus Histone Protein -- 4.2.8 [3Fe-4S] Ferredoxin from Sulpholobus -- 5 Proteins of Medical Interest -- 5.1 Tissue-type Plasminogen Activator -- 5.2 Bcl-XL -- 5.3 ADP Ribosyl Cyclase -- 5.4 Cadherins -- 5.5 Cartilage Oligomeric Protein -- 5.6 Cyclin-dependent Kinase 2/CksHs1 Complex -- 5.7 Cyclin-dependent Kinase/Cyclin-dependent Kinase Inhibitor Complex -- 5.8 Phosphoinositide 3-Kinase p85α Subunit, Breakpoint Cluster Region Homology Domain -- 5.9 Mammalian Phosphoinositide-specific Phospholipase Cδ -- 5.10 Proliferating Cell Nuclear Antigen (Human)/p21 WAF1/C1P1, C-Terminal Fragment Complex -- 5.11 DIG (Disc-large Protein), PDZ Domain -- 5.12 Fibroblast Growth Factor Receptor 1 Tyrosine Kinase (FGFRIK) -- 5.13 α-Hemolysin -- 5.14 HIV Capsid Protein, N-Terminal Core Domain -- 5.15 HIV Matrix Protein -- 5.16 Nef: Regulatory Factor -- 5.17 Human Adenovirus - 2 Endoproteinase/Cofactor Complex -- 5.18 Human Cytomegalovirus Protease -- 5.19 NS3 Protein, Protease Domain, Hepatitis C Virus -- 5.20 Vaccinia H1-related Phosphatase -- 5.21 Vaccinia Virus VP39 -- 5.22 Nuclear Transport Factor -- 5.23 Human p120GAP, GTPase-activating Domain -- 5.24 p53 Tumour Suppressor, Core Domain (Human) S3BP2 Protein, C-terminal Domain (E. coli Complex) -- 5.25 6-Phosphofructo-2-kinase/fructose 2,6-Biphosphate -- 5.26 Inosine 5'-Monophosphate dehydrogenase (IMPDH) -- 5.27 Inosine-Uridine Nucleoside N-Ribohydrolase -- 5.28 Human Kinesin Motor Domain. , 5.29 Yes Kinase Associated Protein, WW Domain (Human)/Peptide Complex.