Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model-Reference-Cited by-同舟云学术

Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model

Published:2016-03-28 Issue:4 Volume:22 Page:
ISSN:1610-2940
Container-title:Journal of Molecular Modeling
language:en
Short-container-title:J Mol Model

Author:

Su Ji-Guo,Han Xiao-Ming,Zhao Shu-Xin,Hou Yan-Xue,Li Xing-Yuan,Qi Li-Sheng,Wang Ji-Hua

Funder

National Natural Science Foundation of China

Natural Science Foundation of Hebei Province

Program for the Outstanding Young Talents of Hebei Province

the funding from Shandong Provincial Key Laboratory of Functional Macromolecular Biophysics

Publisher

Springer Science and Business Media LLC

Subject

Inorganic Chemistry,Computational Theory and Mathematics,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Catalysis

Link

http://link.springer.com/content/pdf/10.1007/s00894-016-2958-4.pdf

Reference61 articles.

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4. Querol E, Perez-Pons JA, Mozo-Villarias A (1996) Analysis of protein conformational characteristics related to thermostability. Protein Eng 9:265–271

5. Sadeghi M, Naderi-Manesh H, Zarrabi M, Ranjbar B (2006) Effective factors in thermostability of thermophilic proteins. Biophys Chem 119:256–270

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