| 查看: 1157 | 回复: 18 | ||||
| 【奖励】 本帖被评价16次，作者wenke1526增加金币 12.4 个 | ||||
[资源]
Theory of Phase Transitions in Polypeptides and Proteins (Springer Theses)2011
|
||||
|
There are nearly 100 000 different protein sequences encoded in the human genome, each with its own specific fold. Understanding how a newly formed polypeptide sequence finds its way to the correct fold is one of the greatest challenges in the modern structural biology. The aim of this thesis is to provide novel insights into protein folding by considering the problem from the point of view of statistical mechanics. The thesis starts by investigating the fundamental degrees of freedom in polypeptides that are responsible for the conformational transitions. This knowledge is then applied in the statistical mechanics description of helix?coil transitions in polypeptides. Finally, the theoretical formalism is generalized to the case of proteins in an aqueous environment. The major novelty of this work lies in comabining (a) a formalism based on fundamental physical properties of the system and (b) the resulting possibility of describing the folding?unfolding transitions quantitatively. The clear physical nature of the formalism opens the way to further applications in a large variety of systems and processes. Common terms and phrases: amino acids degrees of freedom dihedral angles heat capacity molecular dynamics partition function potential energy surface protein folding random coil Cover Springer Theses Theory of Phase Transitions in Polypeptides and Proteins ISBN 9783642227318 Supervisor’s Foreword Acknowledgments Contents 1 Introduction 1.1 Problems Addressed in the Thesis References 2 Theoretical Methods of Quantum Mechanics 2.1 Introduction 2.2 The Schrödinger Equation 2.3 The Born--Oppenheimer Approximation 2.4 Properties of the Wavefunction 2.5 Hartree--Fock Theory 2.6 Density Functional Theory 2.7 Molecular Mechanics Approach: a Way to Overcome the Complexity of Quantum Mechanics References 3 Degrees of Freedom in Polypeptides and Proteins 3.1 Introduction 3.2 Conformational Properties of Alanine and Glycine Chains 3.2.1 Determination of the Polypeptides Twisting Degrees of Freedom 3.2.2 Optimized Geometries of Alanine Polypeptides 3.2.3 Polypeptide Energy Dependance On the Dihedral Angle . 3.2.4 Potential Energy Surface for Alanine Tripeptide 3.2.5 Potential Energy Surface for Alanine Hexapeptide with the Sheet and the Helix Secondary Structure 3.2.6 Comparison of Calculation Results with Experimental Data 3.3 Conformational Changes in Glycine Tri- and Hexa-Peptide 3.3.1 Optimized Geometries of Glycine Polypeptides 3.3.2 Potential Energy Surface for Glycine Tripeptide 3.3.3 Potential Energy Surface for Glycine Hexapeptide with the Sheet and the Helix Secondary Structure 3.3.4 Comparison of Calculation Results with Experimental Data References 4 Partition Function of a Polypeptide 4.1 Introduction 4.2 Molecular Mechanics Potential 4.3 Hamiltonial of a Polypeptide Chain 4.4 Construction of the Partition Function 4.5 Thermodynamical Characteristics of a Polypeptide Chain References 5 Phase Transitions in Polypeptides 5.1 Introduction 5.2 Molecular Dynamics Simulations 5.3 a-HelixRandom Coil Phase Transition in Polyalanine 5.3.1 Accuracy of the Molecular Mechanics Potential 5.3.2 Potential Energy Surface of Alanine Polypeptide 5.3.3 Internal Energy of Alanine Polypeptide 5.3.4 Heat Capacity of Alanine Polypeptide 5.3.5 Calculation of the Zimm--Bragg Parameters 5.3.6 Helicity of Alanine Polypeptides 5.3.7 Correlation of Different Amino Acids in the Polypeptide 5.4 Phase Transitions in Polypeptides: Analysis of Energy Fluctuations 5.4.1 Fluctuations of Internal Energy and Heat Capacity 5.4.2 a-Helix Random Coil Transition in Alanine Polypeptide 5.4.3 p-Helix Random Coil Transition in Valine Polypeptide 5.4.4 p-Helix Random Coil Transition in Leucine Polypeptide 5.4.5 Appendix: Parameters of MD Simulation References 6 Folding of Proteins in Aqueous Environment 6.1 Introduction 6.2 Theoretical Methods 6.2.1 Partition Function of a Protein 6.2.2 Partition Function of a Protein in Water Environment 6.3 Results and Discussion 6.3.1 Heat Capacity of Staphylococcal Nuclease 6.3.2 Heat Capacity of Metmyoglobin References 7 Summary and Conclusions References u08eZUThffEC  [ Last edited by wenke1526 on 2011-12-14 at 11:13 ] |
回复此楼» 本帖附件资源列表
-
欢迎监督和反馈：小木虫仅提供交流平台，不对该内容负责。
本内容由用户自主发布，如果其内容涉及到知识产权问题，其责任在于用户本人，如对版权有异议，请联系邮箱：xiaomuchong@tal.com - 附件 1 : ebooksclub.org__Theory_of_Phase_Transitions_in_Polypeptides_and_Proteins__Springer_Theses_.pdf
2011-12-14 11:13:26, 2.8 M
» 收录本帖的淘帖专辑推荐
 锂电收藏 | 国外专业电子书 |
» 猜你喜欢
使用高温共聚焦原位观察磁场对凝固枝晶的影响
已经有0人回复
-
不同N、Si含量对含钒HRB400e钢组织和性能的影响
已经有0人回复
-
有机高分子材料论文润色/翻译怎么收费?
已经有96人回复
-
深圳大学2026年招聘公告
已经有0人回复
-
中科南京智能技术研究院2026年招聘简章
已经有0人回复
-
匣钵烧结
已经有1人回复
-
超高温激光共聚焦显微镜拓展脉冲磁场装置
已经有0人回复
-
考博求助
已经有0人回复
-
线能量对超高强度海工钢热影响区组织演变与韧性的影响
已经有0人回复
-
【博士招生】材料科学与工程专业（金属类）博士研究生，非诚勿扰。
已经有109人回复
-
使用高温激光共聚焦显微镜原位观察高强度海工钢的贝氏体转变
已经有0人回复
» 本主题相关价值贴推荐，对您同样有帮助:
- [2011-11-20][深圳]第九届全国物理有机化学学术会议
已经有60人回复
- 菜鸟急求Max phase 最基本知识 求各位前辈帮忙！
已经有5人回复
- 【求助】分析柱1.5min出峰，比例不管怎么调出峰时间变化不大？
已经有17人回复
- Journal of Colloid and Interface Science
已经有6人回复
- 【资源】Theory and Experiment in Electrocatalysis
已经有5人回复
- 【求助】Frontiers of Environmental Science and Engineering in China是SCI收录吗？
已经有6人回复
简单回复
2011-12-14 11:14
回复
vaughn3楼
2011-12-14 11:38
回复
三星好评 顶一下，感谢分享！
2011-12-14 11:50
回复
三星好评 顶一下，感谢分享！
zhke5235楼
2011-12-14 15:56
回复
五星好评 顶一下，感谢分享！
2011-12-14 16:28
回复
五星好评 顶一下，感谢分享！
dzb164097楼
2011-12-15 08:59
回复
五星好评 顶一下，感谢分享！ 
lanxzh8楼
2012-05-12 06:24
回复
五星好评 顶一下，感谢分享！
杨寻9楼
2012-11-17 10:05
回复
五星好评 顶一下，感谢分享！
liusheng631110楼
2012-11-22 22:34
回复
五星好评 顶一下，感谢分享！
2012-12-29 16:43
回复
五星好评 顶一下，感谢分享！
2012-12-29 17:22
回复
顶一下，感谢分享！
xiefenxiefen13楼
2013-01-23 20:10
回复
五星好评 顶一下，感谢分享！
jhoo14楼
2013-08-30 16:02
回复
五星好评 顶一下，感谢分享！
一泓山人15楼
2013-09-07 17:01
回复
五星好评 顶一下，感谢分享！
geniuswq16楼
2013-09-24 18:11
回复
五星好评 顶一下，感谢分享！
迷失的羊羔17楼
2013-12-14 08:44
回复
五星好评 顶一下，感谢分享！
ypghnust6118楼
2013-12-20 14:41
回复
五星好评 顶一下，感谢分享！
lerel1234519楼
2019-02-20 17:29
回复
五星好评 顶一下，感谢分享！
