Download Chapter 2 Carbohydrates Chapter 3 Lipids Chapter 4 Amino Acids

三、主要内容与学时安排
章
主要内容及要求
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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
1.4 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
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Chapter 2
Chapter 3
Chapter 4
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Lipids
3.1 Fatty Acids
3.2 Triacylglycerols
3.3 Glycerophospholipids
The most common phospholipids
Ether Glycerophospholipids
3.4 Sphingolipids
3.5 Waxes
3.6 Terpenes
3.7 Steroids
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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
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学时安排
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Amino Acids
4.1 Amino Acids Have Common Structural Features
4.2 Classification of amino acids
Acid-base chemistry of amino acids
Handerson-Hasselbalch 公式：
4.3 Formaldehyde Titration of Amino Acids
4.4 Reactions of Amino Acids
4.5 Spectroscopic Properties of Amino Acids
4.6 Separation and Analysis of Amino Acid Mixtures
4.7 Ion Exchange Chromatography
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Chapter 5
Structure
Proteins：Their Biological functions and Primary
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
5.4 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
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Chapter 6
Structure
Protein: Secondary, Tertiary, and Quaternary
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
6.4 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
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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
7.4 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
7.14 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
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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
8.4 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
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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
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Chapter 10
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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
10.4 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
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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
11.4 Ketone bodies
The formation of ketone bodies
Ketone bodies and diabetes mellitus
The formation and transportation of ketone bodies in hypatocytes.
11.5 Fatty acids biosynthesis
There are four steps in one turn of fatty acids synthesis
Further processing of C16 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
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Chapter 12
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Amino Acid Metabolism
12.1 The nitrogen cycle
12.2 Protein Degradation
Cellular protein degradation
Proteins are ligated for degradation.
12.3 The fate of ammonium-assimilation
Carbamoyl-phosphate synthetase I
Glutamate dehydrogenase (GDH)
Glutamine synthetase
12.4 Amino Acid Biosynthesis
transamination
the pathways of Amino acid biosynthesis
12.5 Metabolic Degradation of Amino Acids
Hereditary defect in amino acids catabolism
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Chapter 13 The Synthesis and Degradation of Nucleotides
13.1 Nucleotide Biosynthesis
13.2 The Biosynthesis of Purines
13.3 Purine Slavage
13.4 Purine degradation
13.5 The Biosynthesis of Pyrimidines
13.6 Pyrimidine degradation
13.7 Deoxyribonucleotide Biosynthesis
13.8 Synthesis of Thymine Nucleotides
Chapter 14
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DNA Replication and Repair
14.1 Three models of DNA replication
14.2 General Features of DNA Replication
Replication is semiconservative
Replication is bidirectional
The replication is semidiscontinuous
14.3 The Enzymes of DNA Replication
DNA polymerase properties
DNA ligase
DNA primase
helicase
DNA single-strand binding protein ( SSB)
DNA gyrase ( topoisomerase)
14.4 The steps of DNA replication
The Initiation of DNA Replication
The Elongation of DNA
The Termination of DNA Replication
14.5 Telomeres and Telomerase
14.6 Reverse Transcription: An RNA-Directed DNA Polymerization
14.7 Polymerase Chain Reaction (PCR)
14.8 Sequencing Nucleic Acids
14.9 DNA Repair
The most common forms of damage:
The common repair systems:
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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
15.4 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
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Chapter 16
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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
16.4 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
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