生物化學(xué)原理

內(nèi)容概要

　　《生物化學(xué)原理(影印版)》因其對(duì)最基本的生物化學(xué)原理進(jìn)行精確、流暢、清晰的描述在國(guó)外受到廣泛的贊揚(yáng)。作者Robert從事生物化學(xué)教學(xué)已30余年，具有豐富的教學(xué)經(jīng)驗(yàn)。全書(shū)共分為四大部分，包括導(dǎo)論、生物大分子的結(jié)構(gòu)和功能、代謝動(dòng)力學(xué)和遺傳物質(zhì)，章節(jié)之間保持較好的連貫性。此版還增加了許多讀者感興趣的內(nèi)容，并闡述了相關(guān)的最新研究進(jìn)展。在每一章后面都附有較全面的練習(xí)題，包括簡(jiǎn)答題、選擇題和論述題，而且在書(shū)后對(duì)練習(xí)題做了詳盡的解答，可以幫助學(xué)生更好地掌握生物化學(xué)基本原理?！　　渡锘瘜W(xué)原理(影印版)》適合生物學(xué)類(lèi)專(zhuān)業(yè)本科學(xué)生和研究生作為雙語(yǔ)教材使用，并可供相關(guān)的研究工作者參考。

作者簡(jiǎn)介

作者：(美國(guó))H.R.Horton (美國(guó))L.A.MoranH.Robert Horton，Dr Horton who received his Ph.D from the University of Missouri in 1962,is William Neal Reynolds rofessor Emeriturs and Alunmi Distinguished Professor Emeritus in the Department of Bisochemistry at North Carolina State University,where he served on the faculty for over 30 years.Most of Professor Hortons research was in protein and enzyme mehanisms.

書(shū)籍目錄

PART ONEIntroduction1 Introduction to Biochemistry2 WaterPART TWOStructure and Function of Biomotecuies3 Amino Acids and the Primary Structures of Proteins4 Proteins: Three-Dimensional Structure and Function5 Properties of Enzymes6 Mechanisms of Enzymes7 Coenzymes and Vitamins8 Carbohydrates9 Lipids and MembranesPART THREEMetabolism and Bioenergetics10 Introduction to Metabolism11 Glycolysis12 The Citric Acid Cycle13 Additional Pathways in Carbohydrate Metabolism14 Electron Transport and Oxidative Phosphorylation15 Photosynthesis16 Lipid Metabolism17 Amino Acid Metabolism18 Nucleotide MetabolismPART FOURBiological Information Flow19 Nucleic Acids20 DNA Replication, Repair, and Recombination21 Transcription and RNA Processing22 Protein Synthesis23 Recombinant DNA TechnologyPART ONEIntrodaction1 Introduction to Biochemistry 31.1 Biochemistry Is a Modem Science41.2 The Chemical Elements of Life 51.3 Many Important Biomolecules Are Polymers 8A. Proteins 8B. Polysaccharides 9C. Nucleic Acids 10D. Lipids and Membranes 121.4 The Energetics of Life 141.5 Biochemistry and Evolution 151.6 The Cell Is the Basic Unit of Life 151.7 Prokaryotic Cells: Structural Features 161.8 Eukaryotic Cells: Structural Features 17A. The Nucleus 17B. The Endoplasmic Reticulum and Golgi Apparatus 19C. Mitochondria and Chloroplasts 19D. Specialized Vesicles 20E. The Cytoskeleton 211.9 A Picture of the Living Cell 211.10 Biochemistry Is Multidisciplinary 23Appendix: The Special Terminology of Biochemistry 23Selected Readings 242 Water 252.1 The Water Molecule Is Polar 262.2 Hydrogen Bonding in Water 272.3 Ionic and Polar Substances Dissolve in Water 282.4 Nonpolar Substances Are Insoluble in Water 292.5 Noncovalent Interactions in Biomolecules 31A. Charge-Charge Interactions 31B. Hydrogen Bonds 31C. Van der Waals Forces 32D. Hydrophobic Interactions 332.6 Water Is Nucleophilic 332.7 Ionization of Water 352.8 The pH Scale 362.9 Acid Dissociation Constants of Weak Acids 372.10 Buffered Solutions Resist Changes in pH40Summary43Problems43Selected Readings45PART TWOStructure and Function of Biornolecules3 Amino Acids and the Primary Structures of Proteins 513.1 General Structure of Amino Acids 52Box 3.1 An Alternative Nomenclature 543.2 Structures of the 20 Common Amino Acids 55A. Aliphatic R Groups 55B. Aromatic R Groups 56C. Sulfur-Containing R Groups 57D. Side Chains with Alcohol Groups 57E. Basic R Groups 58E Acidic R Groups and Their Amide Derivatives 58G. The Hydrophobicity of Amino Acid Side Chains 583.3 Other Amino Acids and Amino Acid Derivatives 593.4 Ionization of Amino Acids 603.5 Peptide Bonds Link Amino Acids in Proteins 643.6 Protein Purification Techniques 663.7 Amino Acid Composition of Proteins 693.8 Determining the Sequence of Amino Acid Residues 703.9 Protein Sequencing Strategies 733.10 Comparisons of the Primary Structures of Proteins Reveal EvolutionaryRelationships 77  Summary 78Problems 79Selected Readings 804 Proteins: Three-Dimensional Structure  and Function 814.1 There Are Four Levels of Protein Structure 834.2 Methods for Determining Protein Structure 844.3 The Conformation of the Peptide Group 864.4 The et Helix 894.5 B Strands and B Sheets 924.6 Loops and Turns 944.7 Tertiary Stacture of Proteins 96A. Supersecondary Structures 96B. Domains 97C. Domain Structure and Function 1024.8 Quaternary Structarc 1024.9 Protein Denaturation and Renaturation 1044.10 Protein Folding and Stability 107A. The Hydrophobic Effect 107B. Hydrogen Bonding 109C. Van der Waals Interactions and Charge-Charge Interactions 1 I0D. Protein Folding Is Assisted by Chaperones 1104.11 Collagen, a Fibrous Protein 1124.12 Structures of Myoglobin and Hemoglobin 1144.13 Oxygen Binding to Myoglobin and Hemoglobin 116A. Oxygen Binds Reversibly to Heine 116B. Oxygen-Binding Curves of Myoglobin and Hemoglobin 117C. Hemoglobin Is an Allosteric Protein l 194.14 Antibodies Bind Specific Antigens 121Summary 124Problems 125Selected Readings 1275 Properties of Enzymes 1305.1 The Six Classes of Enzymes 1315.2 Kinetic Experiments Reveal Enzyme Properties 133A. Chemical Kinetics 133B. Enzyme Kinetics 1345.3 The Michaelis-Menten Equation 135A. Derivation of the Michaclis-Menten Equation 137B. The Meanings of Km 1385.4 Kinetic Constants Indicate Enzyme Activity and Specificity 1395.5 Measurement of Km and V 1405.6 Kinetics of Multisubsate Reactions 1415.7 Reversible Enzyme Inhibition 142A. Competitive Inhibition 143B. Uncompctitive Inhibition 145C. Noncompetitive Inhibition 146D. Uses of Enzyme Inhibition 1465.8 Irreversible Enzyme Inhibition 1475.9 Site-Directed Mutagenesis Modifies Enzymes 1485.10 Regulation of Enzyme Activity 148A. Phosphofructokinase Is an Allosteric Enzyme 149B. Gcnerai Properties of Allostcric Enzymes 150C. Two Theories of Allosteric Regulation 152D. Regulation by Covalent Modification 154……

章節(jié)摘錄

插圖：B. The Endoplasmic Reticulum and Golgi ApparatusA network of membrane sheets and tubules called the endoplasmic reticulum (ER) extends from  the outer membrane of the nucleus. The aqueous region enclosed within the endoplasmic reticulum is called the lumen. In many cells, part of the surface of the endoplasmic reficulum is coated with ribosomes that are actively synthesizing proteins. As synthesis continues, the protein is translocated through the membrane into the lumen. In the case of membrane-spanning proteins, part of the protein remains embedded in the membrane after it is released from the ribosome. Proteins destined for export from the cell are completely extruded through the membrane into the lumen, where they are packaged in membranous vesicles. These vesicles travel through the cell and fuse with the plasma membrane, releasing their contents into the extracellular space. The synthesis of proteins destined to remain in the cytosol occurs at ribosomes that are not bound to the endoplasmic reficulum. Many enzyme systems involved in the metabolism of lipids are concentrated in regions of the endoplasmic reticulum that have no attached ribosomes.In many species, a complex of flattened, fluid-filled, membranous sacs called the Golgi apparatus is often found close to the endoplasmic reticulum and the nucleus. Vesicles that bud off from the endoplasmic reticulum fuse with the Golgi apparatus. The contents of the vesicles may be chemically modified as they pass through the layers of the Golgi apparatus. The modified products are then sorted, packaged in new vesicles, and transported to specific destinations inside or outside the cell.

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