三 主要内容与学时安排 章主要内容及要求学时安排 1 Chapter 1 Introduction to Biochemistry 1.1 Basic concepts of biochemistry 1.2 Biochemistry as a chemical science 1.

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1 三 主要内容与学时安排 章主要内容及要求学时安排 1 Chapter 1 Introduction to Biochemistry 1.1 Basic concepts of biochemistry 1.2 Biochemistry as a chemical science 1.3 Distinction between inanimate matter from living organisms 1. Biological molecules or biomolecules-macromolecules and building blocks 1.5 Biochemistry as an interdisciplinary science 1.6 Biological forces 1.7 Dynamic cells 1.8 Water: the medium of life 2 Chapter 2 Carbohydrates 2.1 Monosaccharides Asymmetric Centers Cyclic Structures Derivatives of Monosaccharides 2.2 Oligosaccharides Disaccharides Higher oligosaccharide 2.3 Polysaccharides Storage Polysaccharides Structural Polysaccharides Glycoprotein 3 Chapter 3 Lipids 3.1 Fatty Acids 3.2 Triacylglycerols 3.3 Glycerophospholipids The most common phospholipids Ether Glycerophospholipids 3. Sphingolipids 3.5 Waxes 3.6 Terpenes 3.7 Steroids Chapter Amino Acids.1 Amino Acids Have Common Structural Features.2 Classification of amino acids Acid-base chemistry of amino acids Handerson-Hasselbalch 公式 :.3 Formaldehyde Titration of Amino Acids. Reactions of Amino Acids.5 Spectroscopic Properties of Amino Acids.6 Separation and Analysis of Amino Acid Mixtures.7 Ion Exchange Chromatography

2 5 Chapter 5 Proteins:Their Biological functions and Primary Structure 5.1 Biological Functions of Proteins Enzymes Regulatory proteins Transport Proteins Storage Proteins Contractile and Motile Proteins Structural Proteins Scaffold Proteins ( Adapter proteins) Protective and Exploitive Proteins 5.2 Polypeptide Are Linear Polymers of Amino Acids 5.3 Peptide classification dipeptide tripeptide tetrapeptide 5. The peptide bond 5.5 Proteins Are Composed of One or More Polypeptide Chains monomeric proteins multimeric proteins 5.6 The Levels of Protein Structure primary structure secondary structure Tertiary structure Quaternary structure 5.7 Protein Conformation Conformation Configuration 5.8 Proteins Have Characteristic Amino Acid Compositions 5.9 Protein Sequencing Strategy Separation of polypeptide chains Cleavage of Disulfide Bridge Analysis of Amino Acid Composition entification of the N- and C-Terminal Residues Fragmentation of the Polypeptide Chain Sequencing Determination of Fragments Reconstruction of the Overall Amino Acid Sequences Location of Disulfide Cross-Bridge 5.10 Related Proteins Share a Common Evolutionary Origin myoglobin hemoglobin 5.11 Solid Phase Peptide Synthesis 5.12 Quantification of Proteins Micro-Kjeldahl Method Lowry Method ( Folin method) BCA Method Coomassie Brilliant Blue Dye Method Ultraviolet Spectrophotometric Method 5.13 Separation Purification and Characterization of Proteins Size exclusion chromatography electrophoresis

3 6 Chapter 6 Protein: Secondary, Tertiary, and Quaternary Structure 6.1 A Protein's Conformation Is Stabilized Largely by Weak Interactions Hydrogen Bonds Hydrophobic Interactions Electrostatic Interactions Van der Waals Interactions 6.2 Secondary Structure in Proteins The Alpha- Helix The Beta-Pleated Sheet 6.3 Fibrous Proteins α- Keratin Fibroin 6. Super-secondary structure αα βαβ ββ 6.5 Globular Proteins and Tertiary Structure Classification of globular proteins 6.6 How Do Proteins Know How to Fold? 6.7 Subunit Interactions and Quaternary Structure 6.8 Protein Structure and Function Myoglobin Hemoglobin

4 7 Chapter 7 Enzyme 7.1 Three distinctive features of enzymes: High catalytic power Specificity Regulation 7.2 Enzyme Nomenclature Formal name Classification number: 7.3 Enzymes and cofactors 7. Enzyme kinetics Enzyme units Michaelis- Menten Equation 7.5 Enzyme-Catalyzed Reactions Involving Two or More Substrate Sequential reactions( 序列反应 ) Ping-Pong reactions 7.6 Effect of activators on enzymatic activity 7.7 Enzyme inhibition the difference between inhibition and inactivation the difference between inreversible inhibition and reversible inhibition 7.8 Catalytic RNA Molecules: Ribozymes 7.9 Catalytic Antibodies: Abyzymes 7.10 Enzyme Specificity and Regulation 7.11 Control over Enzymatic Activity------general considerations 7.12 Zymogens/proenzymes 7.13 Reversible covalent nodification 7.1 The allosteric regulation of enzyme activity 7.15 Glycogen Phosphorylase Allosteric regulation of glycogen phosphorylase Covalent Modification Regulation of Glycogen Phosphorylase 7.16 Enzyme cascade regulation

5 8 Chapter 8 Nucleotides and Nucleic Acids 8.1 The function of nucleic acids 8.2 Nitrogeonous Bases Common Pyrimidines and purines Properties of primidines and purines 8.3 The Pentoses of Nucleotides and Nucleic Acids 8. Nucleotides are nucleoside phosphates 8.5 Nucleic Acids Are Poly-nucleo-tides 8.6 Classes of Nucleic Acids DNA RNA Significance of Chemical Differences Between DNA and RNA 8.7 Hydrolysis of Nucleic Acids Hydrolysis by bases or acids Enzymatic Hydrolysis Restriction Mapping 8.8 The Secondary Structure of DNA B form DNA Z form DNA A form DNA 8.9 Tertiary Structure in DNA Supercoils Cruciforms 8.10 Secondary and Tertiary Structures of RNA 8.11 UV Absorption of Nucleotide and Nucleic Acids 8.12 Denaturation and Renaturation of DNA Denaturation Renaturation 8.13 Nucleic Acid Hybridization Southern Blotting Northern blotting Western blotting 6

6 9 Chapter 9 Carbohydrates Metabolism 9.1 Glycolysis Definition Thermodynamics of Biological Systems The importance of Coupled Reaction in Glycolysis The phases of glycolysis First phase Second phase The metabolic fates of NADH and pyruvate 9.2 The Tricarboxylic Acid Cycle Definition The phases of TCA The fate of carbon atoms of acety-coa in TCA cycle The anaplerotic reactions of TCA cycle Regulation of the TCA cycle 9.3 The glyoxylate cycle of plants and bacteria 10 Chapter 10 Electron Transport and Oxidative Phosphorylation 10.1 The summary of electron transport and electron transfer electron transfer respiratory chain / electron transport chain oxidative phosphorylation 10.2 The members of the electron transport chain Flavoprotein (FP) Coenzyme Q : ubiquinone ( CoQ, UQ ) Cytochromes iron-sulfur proteins (IP) 10.3 Four complexes NADH-coenzyme Q reductase Succinate-coenzyme Q reductase Coenzyme Q cytochrome c reductase Cytochrome c oxidase 10. The Thermodynamic View of Chemiosmotic Coupling 10.5 ATP synthase Binding change mechanism ATP synthase Inhibitors Uncouplers disrupt the coupling of electron transport and ATP synthase ATP exits the mitochondria via an ATP-ADP translocase 10.6 The net yield of ATP from glucose oxidation

7 11 Chapter 11 Lipid Metabolism 11.1 β-oxidation of fatty acids Coenzyme A activates fatty acids by acyl-coa synthetase Carnitine carries fatty acyl groups across the inner mitochondrial membrane The first reaction of β- oxidation The second reaction of β- oxidation The third reaction of β- oxidation The forth of the β- oxidation 11.2 β-oxidation of odd-carbon fatty acids 11.3 β- oxidation of unsaturated fatty acids 11. Ketone bodies The formation of ketone bodies Ketone bodies and diabetes mellitus The formation and transportation of ketone bodies in hypatocytes Fatty acids biosynthesis There are four steps in one turn of fatty acids synthesis Further processing of C 16 fatty acids Biosynthesis of polysaturated fatty acids 11.6 Regulatory control of fatty acid metabolism For catabolism of fatty acids For the synthesis of fatty acids 11.7 Glycerolipid biosynthesis 11.8 Cholesterol Biosynthesis 12 Chapter 12 Amino Acid Metabolism 12.1 The nitrogen cycle 12.2 Protein Degradation Cellular protein degradation Proteins are ligated for degradation The fate of ammonium-assimilation Carbamoyl-phosphate synthetase I Glutamate dehydrogenase (GDH) Glutamine synthetase 12. Amino Acid Biosynthesis transamination the pathways of Amino acid biosynthesis 12.5 Metabolic Degradation of Amino Acids Hereditary defect in amino acids catabolism

8 13 Chapter 13 The Synthesis and Degradation of Nucleotides 13.1 Nucleotide Biosynthesis 13.2 The Biosynthesis of Purines 13.3 Purine Slavage 13. Purine degradation 13.5 The Biosynthesis of Pyrimidines 13.6 Pyrimidine degradation 13.7 Deoxyribonucleotide Biosynthesis 13.8 Synthesis of Thymine Nucleotides 2 1 Chapter 1 DNA Replication and Repair 1.1 Three models of DNA replication 1.2 General Features of DNA Replication Replication is semiconservative Replication is bidirectional The replication is semidiscontinuous 1.3 The Enzymes of DNA Replication DNA polymerase properties DNA ligase DNA primase helicase DNA single-strand binding protein ( SSB) DNA gyrase ( topoisomerase) 1. The steps of DNA replication The Initiation of DNA Replication The Elongation of DNA The Termination of DNA Replication 1.5 Telomeres and Telomerase 1.6 Reverse Transcription: An RNA-Directed DNA Polymerization 1.7 Polymerase Chain Reaction (PCR) 1.8 Sequencing Nucleic Acids 1.9 DNA Repair The most common forms of damage: The common repair systems:

9 15 Chapter 15 Transcription 15.1 The difference between replication and transcription 15.2 E. Coli RNA Polymerase 15.3 The steps of transcription in E. coli Initiation of polymerization Chain elongation Chain termination 15. The RNA polymerase of Eukaryotic Cell 15.5 Transcription Regulation in Prokaryotes operon operator repressor inducer 15.6 Post-transcription Processing in Eukaryotes Split gene 15.7 Post-transcriptional processing of pre-mrna Capping and methylation 3 -polyadenylation Nuclear pre-mrna splicing 16 Chapter 16 Protein Synthesis 16.1 The genetic code The common natures of the genetic code: Elucidating the genetic code 16.2 Codon- anticodon paring The purpose of wobble 16.3 The second genetic code: Amino-tRNA synthetase recognition of proper substrates 16. Ribosome Structure and Assembly 16.5 The mechanics of Protein Synthesis Peptide chain initiation Peptide Chain Elongation Peptide Chain Termination 16.6 Inhibitors of Protein Synthesis