Title Biochemistry
Author T. A. Brown
ISBN 9789387153523
List price Rs 995.00
Price outside India Available on Request
Original price
Binding Paperback
No of pages 564
Book size 216 x 279 mm
Publishing year 2018
Original publisher Scion Publishing Limited
Published in India by Viva Books Private Limited
Exclusive distributors Viva Books Private Limited
Sales territory India, Sri Lanka, Bangladesh, Pakistan, Nepal, .
Status New Arrival
About the book

Preamble and Practice Tutorial Numerical Problems by
S. N. Mukhopadhyay

Biochemistry by Terry Brown was conceived and written exclusively for introductory courses and is the ideal way to understand and learn this fascinating subject, whatever your background. It covers the key biochemical principles you will need to know whilst providing sufficient detail to allow a full appreciation of the subject.

Writing in the clear and concise style for which he is renowned, the author guides you through:

• the cells, organisms and basic biomolecules that are central to biochemistry

• the generation of energy and the key elements of metabolism

• the storage and reproduction of biological information, including DNA repair, protein synthesis and the control of gene expression

This edition has been designed for students and scholars in the Indian subcontinent specially keeping in view the course curricula in universities and other biochemistry courses. To make the book more user-friendly additional chapter-wise practice tutorial numerical problems have been included.

The book concludes with chapters describing the techniques used to study proteins, lipids and carbohydrates as well as DNA and RNA.

The book includes a number of features to help you understand the subject:

• the basic principles are reinforced through real-world examples and applications

• key concepts in chemistry are detailed in separate boxes

• self-assessment questions in a variety of formats allow you to test your understanding

• practice tutorial numerical problems

Biochemistry – a concise and accessible text for students taking a course in biochemistry.





How to use this book

Chapter 1: Biochemistry in the modern world • What is biochemistry? • Chemistry is also important in biochemistry • Box 1.1 The origins of biochemistry • Box 1.2 Schrödinger and biology • Biochemistry involves the study of very large biomolecules • Box 1.3 Atoms, isotopes and molecular masses • Biochemistry is also the study of metabolism • The storage and utilization of biological information is an important part of biochemistry • Biochemistry is an experimental science • Box 1.4 Omes are collections of biomolecules • Further reading

PART 1: Cells, organisms and biomolecules

Chapter 2: Cells and organisms • Cells the building blocks of life • Box 2.1 Units of measurement • There are two different types of cell structure • Box 2.2 Species names • Prokaryotes • Box 2.3 Bacteria communicate with one another in a biofilm • Box 2.4 The microbiome • Eukaryotes • What about viruses? • Box 2.5 Unusual types of infectious particles • Evolution and the unity of life • Life originated four billion years ago • Three and a half billion years of evolution • Box 2.6 Mass extinction events • Further reading • Self-assessment questions

Chapter 3: Proteins • Proteins are made of amino acids • Twenty different amino acids are used to make proteins • The biochemical features of amino acids • Box 3.1 Are there two versions of every amino acid? • Box 3.2 The ionization of water and the pH scale • Some amino acids are modified after protein synthesis • Box 3.3 Types of chemical bond • The primary and secondary levels of protein structure • Polypeptides are polymers of amino acids • Polypeptides can take up regular conformations • Box 3.4 The unusual characteristics of the peptide bond • Box 3.5 What is the difference between a left-handed and a right-handed helix? • Box 3.6 Predicting the secondary structure of polypeptide from its amino acid sequence • Fibrous and globular proteins • Fibrous proteins: keratin, collagen and silk • Globular proteins have tertiary and possibly quaternary structures • Box 3.7 Using collagen structure to identify extinct animals • Box 3.8 An example of a protein with a mixture of domains • Protein folding • Small proteins fold spontaneously into their correct tertiary structures • Protein folding pathways • Box 3.9 Studying protein folding • Protein folding is one of the fundamental principles of biology • Further reading • Self-assessment questions

Chapter 4: Nucleic acids • The structures of DNA and RNA • Polynucleotide structure • DNA and RNA secondary structures • Box 4.1 Base stacking • Box 4.2 The discovery of the double helix • Box 4.3 Sugar pucker • Box 4.4 Units of length for nucleic acid molecules • RNAs display a diverse range of chemical modifications • Packaging of DNA • Nucleosomes and chromatin fibers • Box 4.5 DNA packaging in bacteria • Further reading • Self-assessment questions

Chapter 5: Lipids and biological membranes • Lipid structures • Fatty acids and their derivatives • Box 5.1 Structural notation for fatty acids • Box 5.2 Essential fatty acids • Diverse lipids with diverse functions • Box 5.3 Polyterpenes • Box 5.4 Prostaglandins • Biological membranes • Membrane structure • Box 5.5 The carbohydrate component of a membrane • Membranes as selective barriers • Box 5.6 Voltage-gated ion channels and nerve impulses • Box 5.7 The biochemistry of cystic fibrosis • Further reading • Self-assessment questions

Chapter 6: Carbohydrates • Monosaccharides, disaccharides and oligosaccharides • Monosaccharides are the building blocks of carbohydrates • Box 6.1 Representations of monosaccharide structures • Box 6.2 The different types of isomers relevant to carbohydrate structure • Disaccharides are made by linking together pairs of monosaccharides • Box 6.3 Some humans have recently evolved the ability to digest milk • Oligosaccharides are short monosaccharide polymers • Polysaccharides • Starch, glycogen, cellulose and chitin are homopolysaccarides • Box 6.4 The reducing and non-reducing ends of a starch molecule • Heteropolysaccharides are found in the extracellular matrix and in bacterial cell walls • Further reading • Self-assessment questions

PART 2: Energy generation and metabolism

Chapter 7: Enzymes • What is an enzyme? • Most enzymes are proteins • Some enzymes require cofactors • Box 7.1 Metalloproteins and metalloenzymes • Enzymes are classified according to their function • Box 7.2 Oxidation and reduction reactions • How enzymes work • Enzymes are biological catalysts • Box 7.3 Reversible reactions • Box 7.4 The specificity of substrate binding • Factors influencing the rate of an enzyme-catalyzed reaction • Box 7.5 Exploiting thermostable enzymes in biofuel production • Box 7.6 The Michaelis–Menten equation Inhibitors and their effects on enzymes • Box 7.7 Allosteric enzymes • Further reading • Self-assessment questions

Chapter 8: Energy generation: glycolysis • An overview of energy generation • Box 8.1 Units of energy • Activated carrier molecules store energy for use in biochemical reactions • Biochemical energy generation is a two-stage process • Glycolysis • The glycolytic pathway • Box 8.2 Biochemical synthesis of ATP • Glycolysis in the absence of oxygen • Box 8.3 Aerobes and anaerobes • Glycolysis starting with sugars other than glucose • Regulation of glycolysis • Box 8.4 Why is phosphofructokinase regulated by AMP and not ADP? • Box 8.5 Control of fructose 6-phosphate levels by glucagon • Further reading • Self-assessment questions

Chapter 9: Energy generation: the TCA cycle and electron transport chain • The TCA cycle • The entry of pyruvate into the TCA cycle • Box 9.1 Identification of the mitochondrial pyruvate carrier protein • The steps of the TCA cycle • Box 9.2 Succinyl CoA synthetases • Regulation of the TCA cycle • The electron transport chain and the synthesis of ATP • Energy is released as electrons are passed along the electron transport chain • Box 9.3 Redox potential • The structure and function of the electron transport chain • Box 9.4 The location of the electron transport chain • Synthesis of ATP • Box 9.5 Why is a protein that makes ATP called an ATPase? • Box 9.6 The rotation of the F0F1 ATPase • Inhibitors and uncouplers of the electron transport chain • Cytoplasmic NADH cannot gain access to the electron transport chain • Box 9.7 The smell of skunk cabbage • Further reading • Self-assessment questions

Chapter 10: Photosynthesis • An overview of photosynthesis • Photosynthesis is the light-driven production of carbohydrates • Photosynthesis occurs in specialized organelles • The light reactions • Sunlight is harvested by photosynthetic pigments • Box 10.1 Fall colors • Box 10.2 Atomic orbitals • Box 10.3 The role of carotenoid pigments in photoprotection • Electron transport and photophosphorylation • Box 10.4 The Z scheme • Box 10.5 Photosynthesis in bacteria • The dark reactions • The Calvin cycle • Synthesis of sucrose and starch • Carbon fixation by C4 and CAM plants • Box 10.6 Increasing the photosynthetic capability of crop plants • Further reading • Self-assessment questions

Chapter 11: Carbohydrate metabolism • Glycogen metabolism • Synthesis and degradation of glycogen • Control of glycogen metabolism • Box 11.1 Blood sugar • Box 11.2 Avoiding a futile cycle • Box 11.3 Control of glycogen metabolism by calcium • Box 11.4 Allosteric control of glycogen metabolism in liver cells • Gluconeogenesis • The gluconeogenesis pathway • Box 11.5 The energy budget for gluconeogenesis • Regulation of gluconeogenesis • The pentose phosphate pathway • The oxidative and non-oxidative phases of the pentose phosphate pathway • Box 11.6 Did Pythagoras ban the broad bean because of the pentose phosphate pathway? • Further reading • Self-assessment questions

Chapter 12: Lipid metabolism • Synthesis of fatty acids and triacylglycerols • Fatty acid synthesis • Box 12.1 The energy requirement for fatty acid synthesis • Triacylglycerol synthesis • Box 12.2 Lipoproteins • Breakdown of triacylglycerols and fatty acids • Breakdown of triacylglycerols into fatty acids and glycerol • Breakdown of fatty acids • Box 12.3 The Greek notation for fatty acid structure • Box 12.4 The glyoxylate cycle • Box 12.5 The biochemistry of Lorenzo’s Oil • Synthesis of cholesterol and its derivatives • Synthesis and degradation of cholesterol • Synthesis of cholesterol derivatives • Further reading • Self-assessment questions

Chapter 13: Nitrogen metabolism • Synthesis of ammonia from inorganic nitrogen • Nitrogen fixation • Box 13.1 Nitrogen fixation by symbiotic cyanobacteria • Nitrate reduction • Synthesis of nitrogen containing biochemicals • Synthesis of amino acids • Box 13.2 Synthesis of the correct enantiomer of glutamate • Box 13.3 Genetically modified crops that are resistant to a herbicide that disrupts aromatic amino acid synthesis • Synthesis of nucleotides • Box 13.4 Nucleotide synthesis is a target for cancer chemotherapy • Tetrapyrrole synthesis • Degradation of nitrogen-containing compounds • Degradation of amino acids • The urea cycle • Box 13.5 Diseases associated with defects in nitrogen metabolism • Further reading • Self-assessment questions

PART 3: Storage of biological information and synthesis of proteins

Chapter 14: DNA replication and repair • DNA replication • Initiation of DNA replication • The elongation phase of DNA replication • Box 14.1 Supercoiled DNA • Box 14.2 DNA polymerases • Box 14.3 Why does a DNA polymerase require a primer? • Termination of replication • Box 14.4 The interaction between Tus proteins and the replisome • Box 14.5 Telomerase and cancer • DNA repair • Correcting errors in DNA replication • Box 14.6 Base tautomerism can result in replication errors • Repair of damaged nucleotides • Box 14.7 Photoreactivation repair of cyclobutyl dimers • Box 14.8 Defects in DNA repair underlie a number of important human diseases • Repair of DNA breaks • Further reading • Self-assessment questions

Chapter 15: RNA synthesis • Transcription of DNA into RNA • Coding and noncoding RNAs • Initiation of transcription • Box 15.1 Promoters for RNA polymerase I and RNA polymerase III • The RNA synthesis phase of transcription • Box 15.2 Rifamycins are important antibiotics that block bacterial RNA synthesis • Termination of transcription • RNA processing • Processing of noncoding RNA by cutting and end-trimming • Box 15.3 Density gradient centrifugation • Removal of introns from eukaryotic pre-mRNA • Box 15.4 Transesterification • Box 15.5 The ‘minor spliceosome’  • Box 15.6 Alternative splicing • Chemical modification of noncoding RNA • Further reading • Self-assessment questions

Chapter 16: Protein synthesis • The genetic code • The features of the genetic code • How the genetic code is enforced during protein synthesis • Box 16.1 The notation for distinguishing between different tRNAs • Box 16.2 Wobble and alternative initiation codons • The mechanics of protein synthesis • Ribosomes • Translation of an mRNA into a polypeptide • Box 16.3 Internal ribosome entry sites – initiation of eukaryotic translation without scanning • Box 16.4 Antibiotics that target the bacterial ribosome • Post-translational processing of proteins • Processing by proteolytic cleavage • Box 16.5 Synthesis of the Gag and Gag–Pol polyproteins • Chemical modification of proteins • Protein targeting • The role of sorting sequences in protein targeting • Box 16.6 Protein targeting in bacteria • Further reading • Self-assessment questions

Chapter 17: Control of gene expression • Regulation of the gene expression pathway • Regulation of the initiation of transcription in bacteria • Box 17.1 Transcriptomics – studying changes in gene expression patterns • Box 17.2 The allolactose paradox • Box 17.3 Repressible operons • Regulation of the initiation of transcription in eukaryotes • Box 17.4 Zinc fingers • Gene regulation after transcript initiation • Degradation of mRNA and protein • RNA degradation • Degradation of proteins • Box 17.5 Protein and mRNA half-lives • Further reading • Self-assessment questions

PART 4: Studying biomolecules

Chapter 18: Studying proteins, lipids and carbohydrates • Methods for studying proteins • Methods for identifying the presence of an individual protein • Box 18.1 Immunoglobulins and antibody diversity • Box 18.2 Electrophoresis • Studying a proteome • Box 18.3 Chromatography • Studying the structure of a protein • Box 18.4 Circularly polarized light • Box 18.5 Interpreting an NMR spectrum • Studying lipids and carbohydrates • Box 18.6 Metabolomics • Methods for studying lipids • Studying carbohydrates • Further reading • Self-assessment questions

Chapter 19: Studying DNA and RNA • Manipulation of DNA and RNA by purified enzymes • Types of enzyme used to study DNA and RNA • Box 19.1 What is ‘restriction’? • The polymerase chain reaction • Box 19.2 Using PCR to alter the codons in a gene • DNA sequencing • Methodology for DNA sequencing • Next generation sequencing • Box 19.3 Did Neanderthals and modern humans meet and interbreed? • DNA cloning • Methods for DNA cloning • Box 19.4 Integration of a yeast plasmid into a chromosome • Using DNA cloning to obtain recombinant protein • Box 19.5 Synthesis of recombinant factor VIII protein • Further reading • Self-assessment questions

Practice tutorial numerical problems



About the Author:

T. A. Brown - University of Manchester, UK.

Target Audience:

Students and academicians of Biochemistry.


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