Analysis of oligomeric proteins during unfolding by pH and temperature

被引：0
|
作者：
Pradip Bhattacharya
Tamil Ganeshan
Soumiyadeep Nandi
Alok Srivastava
Prashant Singh
Mohommad Rehan
Reshmi Rashkush
Naidu Subbarao
Andrew Lynn
机构：
[1] Jawaharlal Nehru University,School of Life Sciences
[2] Jawaharlal Nehru University,School of Information Technology
来源：
Journal of Molecular Modeling | 2009年 / 15卷
关键词：
Analysis of structure and conformation at various pH; Binding free energy; Docking; Electrostatic charge of protein; Free energy; Molecular dynamic simulation; Oligomeric proteins; Unfolding of proteins; Variation of pH and temperature;
D O I：
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中图分类号：
学科分类号：
摘要：
During thermal transition and variation of pH, structural properties of 35 proteins and their complexes (bound with substrate and co-factor) were analyzed in detail. During pH alteration, these proteins were shown to have substantial differences in conformations. pH conformers were analyzed in detail. Free energy and other energy parameters were also estimated for these proteins at various pH and temperatures. Detailed structural analysis and binding interfaces of various substrates, inhibitors and cofactor of these proteins were also investigated using docking and molecular dynamic simulation.
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页码：1013 / 1025
页数：12
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