Literature DB >> 21142237

Is stoichiometry-driven protein folding getting out of thermodynamic control?

Xing-Lai Ji1, Shu-Qun Liu.   

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Year:  2011        PMID: 21142237     DOI: 10.1080/07391102.2011.10508598

Source DB:  PubMed          Journal:  J Biomol Struct Dyn        ISSN: 0739-1102


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  3 in total

1.  Insights into the role of electrostatics in temperature adaptation: a comparative study of psychrophilic, mesophilic, and thermophilic subtilisin-like serine proteases.

Authors:  Yuan-Ling Xia; Jian-Hong Sun; Shi-Meng Ai; Yi Li; Xing Du; Peng Sang; Li-Quan Yang; Yun-Xin Fu; Shu-Qun Liu
Journal:  RSC Adv       Date:  2018-08-22       Impact factor: 4.036

2.  Effect of the Solvent Temperatures on Dynamics of Serine Protease Proteinase K.

Authors:  Peng Sang; Qiong Yang; Xing Du; Nan Yang; Li-Quan Yang; Xing-Lai Ji; Yun-Xin Fu; Zhao-Hui Meng; Shu-Qun Liu
Journal:  Int J Mol Sci       Date:  2016-02-19       Impact factor: 5.923

3.  Protein dynamics and motions in relation to their functions: several case studies and the underlying mechanisms.

Authors:  Li-Quan Yang; Peng Sang; Yan Tao; Yun-Xin Fu; Ke-Qin Zhang; Yue-Hui Xie; Shu-Qun Liu
Journal:  J Biomol Struct Dyn       Date:  2013-03-25
  3 in total

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