《生物统计学》求取 ⇩

第1章 绪论1

Chapter 1 Introduction1

Chapter 2Fundamentals of Molecular Structure of Proteins4

2.1 蛋白质的生物学功能4

第2章蛋白质分子的结构基础4

2.1 Biological Function of Proteins4

2.2 蛋白质分子的化学结构5

2.2 Chemical Structure of Proteins5

2.3 蛋白质分子的空间结构11

2.3 Three-Dimensional Structure of proteins11

参考文献18

References18

第3章蛋白质侧链基团的修饰反应19

3.1 特定的氨基酸残基侧链基团的反应试剂19

3.1 Specific Reagents of Modification Reaction of Amino Acid Residues19

Chapter 3Modification of Side Chain Groups of Proteins19

3.2 巯基的化学修饰22

3.2 The Modification of Thiol Groups22

3.3 氨基的化学修饰26

3.3 The Modification of Amino Groups26

3.4 羰基的化学修饰30

3.4 The Modification of Carboxyl Groups30

3.5 The Modification of Imidazole Groups32

3.5 咪唑基的化学修饰32

3.6 The Modification of Enol and Hydroxyl Groups34

3.6 酚和脂肪族羟基的化学修饰34

3.7 The Modification of Guanidine Groups35

3.7 胍基的化学修饰35

3.8 吲哚基的化学修饰38

3.8 The Modification of Indole Groups38

3.9 硫醚基的化学修饰40

3.9 The Modification of Thioether Groups40

3.10 二硫键的化学修饰41

3.10 The Modification of Disulfides Groups41

3.11 化学修饰反应条件的影响43

3.11 Effects of Reaction Conditions on Modification43

References46

参考文献46

4.1 Ray-Koshland s Method50

Chapter 4Quantitative Treatment of Protein Chemical Modification50

4.1 Ray-Koshland方法50

第4章蛋白质化学修饰的定量处理50

4.2 邹承鲁作图法52

4.2 Tsou s Method52

References61

参考文献61

Chapter 5Kinetics of Chemical Modification of Enzymes63

5.1 Principles of Kinetics of Chemical Modification63

5.1 酶化学修饰的动力学机制63

第5章酶的化学修饰动力学63

5.2 Determination of Enzyme-Ligand Dissociation Constant Using Kinetic Method65

5.2 利用失活动力学确定酶配体解离常数65

5.3 Kinetics of Substrate Reaction during Modification of Enzymes69

5.3 酶活性修饰过程中底物反应动力学69

5.4 不可逆抑制动力学在其它方面的应用82

5.4 Applications of Kinetiks of Irreversible Inhibition in the Other Research Field82

References86

参考文献86

6.1 Affinity Labcling89

Chapter 6 Site-Specific Chemical Modification of Proteins89

第6章蛋白质的位点专一性修饰89

6.1 亲和标记89

6.2 Light-Affinity Labeling96

6.2 光亲和标记96

6.3 蛋白质分子中特定部位的专一性荧光标记102

6.3 Fluorescence Labeling at Specific Sites of Protein Molecules102

6.4 蛋白质专一性标记在探测酶的活性部位构象变化上的应用110

6.4 Site-Specific Labeling Applied to Explore the Conformational Changes at the Active Site of Enzy110

References115

参考文献115

Chapter 7Chemical Cross-Linking of Peptide Chains118

7.1 Cleavable and Incleavable Cross-Linking118

7.1 不可切断的和可切断的化学交联118

第7章蛋白质的化学交联和化学偶联118

7.2 Light-Affinity Cross-Linking122

7.2 蛋白质的光亲和交联122

7.3 蛋白质分子的固定化125

7.3 Immobilization of Proteins125

References129

参考文献129

Chapter 8Site-Directed Mutagenesis-Chemical Modification of Main Chain Structure of Proteins131

8.1 Deletion and Insertion of Genes131

8.1 基因的缺失和插入131

第8章基因定点诱变--蛋白质主链结构的化学修饰131

8.2 Site-Directed Mutagenesis by Oligonucleotide135

8.2 寡聚核苷酸介导的定点诱变135

References140

参考文献140

Appendix Ⅰ Some Commonly Used Reagents for Chemical Modification in Proteins141

附录1 各种修饰试剂对蛋白质侧链基团的反应性141

Appendix Ⅱ Mathematical ???ustration of Tsou plot150

附录2邹承鲁作图法的数学证明150

References155

参考文献155

Appendix Ⅲ Quantitative Relation between Modification of Functional Groups of Proteins and Their B156

附录3蛋白质功能基团的修饰与其生物活力之间的定量关系--计算机模拟确定必需基团的数目和性质156

References163

参考文献163