Chemistry of natural products : amino acids, peptides, proteins, and enzymes

Library	Item Barcode	Call Number	Material Type	Item Category 1	Status
Searching... IBD Library	30000010042325	QD431 A34 2006	Open Access Book	Book	Searching... Unknown
Searching... PSZ JB	30000010172639	QD431 A34 2006	Open Access Book	Book	Searching... Unknown

This volume deals with amino acids, peptides, proteins and enzymes.
The text is divided into four chapters: a chapter each dedicated
to amino acids, peptides, proteins and enzymes respectively. The first chapter on 'Amino Acids' covers their nomenclature, classification, stereo-chemistry, physical and chemical properties, synthesis and industrial applications. The important reactions have been explained with the help of the mechanisms involved. The second chapter on 'Peptides' explains the formation and structure of the peptide bond and its significance. The chapter gives a detailed account of the solution phase and solid phase synthesis of peptides as well as discussing the structure and function of some biologically important peptides. The next chapter on 'Proteins' discusses different types of classification and explains their properties. The structural organisation of proteins has been covered in detail including the primary structure determination. The fourth and the last chapter on 'Enzymes' is a logical extension of the coverage in the first three chapters. It covers the classification, nomenclature and mode of action of enzymes, and a detailed account of the structure and function of different coenzymes.

Author Notes

V.K.Ahluwalia is visiting professor at Dr. B.R. Ambedkar center for Biomedical Research, University of Delhi
Lalita. S. Kumar is working as Reader at Indira Gandhi National Open University (IGNOU), New Delhi
Sanjiv Kumar is working as Reader at Deshbandhu College, University of Delhi

Reviews 1

Choice Review

Where does one begin in criticizing this book? First, the title is misleading. This book is solely about proteins and their constituent building blocks. "Natural products" is a term reserved for smaller metabolites. The book was purportedly written with biochemistry students in India as the target audience. Students using this book will be woefully underprepared for modern protein chemistry. The material presented was discussed in biochemistry courses in the 1970s. The representations of one form of ionized amino acids on pages 21, 26, and 27 are totally wrong. In addition, the days of tasting chemicals are over. There is very little new material in the book and what is presented is often inaccurate. One cannot determine the mass of proteins using ESI MS/MS. There is no mention of peptide synthesis resins, spectroscopic methods for determining structure of proteins, and enzymes functioning in non-aqueous solvents. What the book does show is how biochemistry was in the past, so from a historical perspective it may be somewhat useful. Summing Up: Not recommended. J. M. Tomich Kansas State University

Preface	p. v
Chapter -1 Amino Acids
1.1 Introduction	p. 1
1.2 Nomenclature of Amino Acids	p. 2
1.2.1 Representation of Amino Acids	p. 5
1.3 Classification of Amino Acids	p. 7
1.3.1 Coded or Primary Protein Amino Acids	p. 7
1.3.1.1 Nonpolar or Apolar Amino Acids	p. 7
1.3.1.2 Neutral or Uncharged Polar Amino Acids	p. 9
1.3.1.3 Charged Polar Amino Acids	p. 10
1.3.2 Secondary and Tertiary Protein Amino Acids	p. 11
1.3.3 Non-Coded or Non-Protein Amino Acids	p. 13
1.3.4 Essential Amino Acids	p. 14
1.4 Stereochemical Aspects of [alpha]-Amino Acids	p. 15
1.4.1 Absolute Configuration of [alpha]-Amino Acids	p. 16
1.4.1.1 The RS Notation	p. 17
1.4.2 Amino Acids with Two Chiral Centres	p. 18
1.5 Physical Properties of [alpha]-Amino Acids	p. 20
1.5.1 General Physical Properties	p. 20
1.5.2 Acid-Base Properties of Amino Acids	p. 21
1.5.2.1 Amino Acids with Non -Ionisable Side Chains	p. 22
1.5.2.2 Amino Acids with Ionisable Side Chains	p. 25
1.5.3 Spectral Properties of [alpha]-Amino Acids	p. 28
1.5.3.1 Mass Spectrometry	p. 28
1.5.3.2 Nuclear Magnetic Resonance (NMR) Spectroscopy	p. 29
1.5.3.3 UV Spectroscopy	p. 31
1.5.3.4 IR Spectroscopy	p. 31
1.5.3.4 Circular Dichroism (CD)	p. 32
1.6 Chemical Reactions of Amino Acids	p. 32
1.6.1 Reactions due to Amino Group	p. 32
1.6.2 Reactions due to Carboxyl Group	p. 35
1.6.3 Reactions due to both Amino and Carboxyl Groups	p. 36
1.7 Industrial Preparation of [alpha]-Amino Acids	p. 39
1.8 Chemical Synthesis of [alpha]-Amino Acids	p. 40
1.8.1 Enantiomeric Resolution of [alpha]-Amino Acids	p. 50
1.8.2 Asymmetric Synthesis of [alpha]-Amino Acids	p. 53
1.9 Industrial Applications of [alpha]-Amino Acids	p. 62
Exercises	p. 64
Chapter -2 Peptides
2.1 Introduction	p. 67
2.2 Structure and Classification of Peptides	p. 68
2.2.1 Structure of Peptide Bond	p. 68
2.2.2 Classification of Peptides	p. 71
2.3 Nomenclature of Peptides	p. 72
2.3.1 Representation of Peptides and Polypeptides	p. 73
2.4 Peptide Synthesis	p. 74
2.4.1 Protection of Amino Group	p. 78
2.4.2 Protection of Carboxyl Group	p. 86
2.4.3 Protection of Side Chains	p. 87
2.4.4 Coupling Methods	p. 88
2.5 Solid Phase Peptide Synthesis	p. 95
2.5.1 Solid Phase Peptide Synthesis using t-Boc Protection (Merrifield Approach)	p. 98
2.5.2 Solid Phase Peptide Synthesis using Fmoc Protection (Sheppard's Approach)	p. 99
2.5.3 Limitations of Solid Phase Peptide Synthesis	p. 101
2.6 Some Biologically Important Peptides	p. 103
2.6.1 Oxytocin	p. 103
2.6.2 Glutathione	p. 105
2.6.2.1 Role of Glutathione in Disulphide Bond Formation	p. 106
2.6.2.2 Role of Glutathione as an Antioxidant	p. 107
2.6.3 Insulin	p. 108
2.6.3.1 Structure Determination of Insulin	p. 108
2.6.3 Bradykinin	p. 109
2.6.4 Gramicidin	p. 110
Exercises	p. 112
Chapter -3 Proteins
3.1 Introduction	p. 113
3.2 Classification of Proteins	p. 114
3.2.1 Classification on the Basis of Shape and Structure	p. 114
3.2.2 Classification on the Basis of Products of Hydrolysis	p. 116
3.2.3 Classification on the Basis of Biological Functions	p. 121
3.3 Properties of Proteins	p. 122
3.3.1 Molecular Weight	p. 122
3.3.2 Amphoteric Nature	p. 123
3.3.3 Solubility	p. 124
3.3.4 Precipitation	p. 125
3.3.5 Denaturation	p. 126
3.3.6 Colour Reactions	p. 126
3.4 Structural Organisation of Proteins	p. 131
3.4.1 Covalent or Primary Structure of Proteins	p. 131
3.4.1.1 Amino Acid Composition of Proteins	p. 131
3.4.1.2 Amino Acid Sequence of Polypeptides	p. 134
3.4.2 Conformational Aspects of Proteins: Higher Order Structures	p. 147
3.4.2.1 Secondary Structure of Proteins	p. 147
3.4.2.2 Tertiary Structure of Proteins	p. 157
3.4.2.3 Quaternary Structure of Proteins	p. 158
Exercises	p. 160
Chapter -4 Enzymes
4.1 Introduction	p. 163
4.2 Nomenclature and Classification of Enzymes	p. 164
4.2.1 Systematic and Recommended Names	p. 165
4.2.2 Classification Numbers and Code Names	p. 165
4.3 Characteristics of Enzymes	p. 173
4.3.1 Catalytic Power	p. 173
4.3.2 Enzyme Specificity	p. 173
4.3.3 Enzyme Regulation	p. 175
4.4 Mechanism of Enzyme Action	p. 176
4.5 Factors Affecting Enzyme Action	p. 179
4.6 Chymotrypsin: An Enzyme in Action	p. 182
4.6.1 Structure of Chymotrypsin	p. 182
4.6.2 Important Amino Acid Residues of Chymotrypsin	p. 184
4.6.3 Mechanism of Action	p. 186
4.7 Cofactors (or Coenzymes)	p. 190
4.7.1 Nicotinamide Adenine Dinucleotide (NAD[superscript +]) and Nicotinamide Adenine Dinucleotide Phosphate (NADP[superscript +])	p. 192
4.7.2 UDP-Glucose	p. 195
4.7.3 Flavin Mononucleotide (FMN) and Flavin Adenine Dinucleotide (FAD)	p. 197
4.7.4 Thiamine Pyrophosphate (TPP)	p. 200
4.7.5 CoCarboxylase	p. 202
4.7.6 Pyridoxal-5-Phosphate	p. 205
4.8 Enzymes in Organic Synthesis	p. 210
4.8.1 Enzymatic Oxidations	p. 212
4.8.2 Enzymatic Hydroxylation	p. 214
4.8.3 Enzymatic Hydrolysis	p. 214
4.8.4 Enzymatic Reductions	p. 215
4.8.5 Enzymatic Isomerisations	p. 217
4.6.6 Pharmaceutical Applications of Enzymes	p. 217
Exercises	p. 219
Glossary	p. 221
Index	p. 237

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Author Notes

Reviews 1

Choice Review

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