Crystal structure of Bacillus fastidious uricase reveals an unexpected folding of the C-terminus residues crucial for thermostability under physiological conditions-Reference-Cited by-同舟云学术

Crystal structure of Bacillus fastidious uricase reveals an unexpected folding of the C-terminus residues crucial for thermostability under physiological conditions

Published:2015-03-20 Issue:19 Volume:99 Page:7973-7986
ISSN:0175-7598
Container-title:Applied Microbiology and Biotechnology
language:en
Short-container-title:Appl Microbiol Biotechnol

Author:

Feng Juan,Wang Lu,Liu Hongbo,Yang Xiaolan,Liu Lin,Xie Yanling,Liu Miaomiao,Zhao Yunsheng,Li Xiang,Wang Deqiang,Zhan Chang-Guo,Liao Fei

Publisher

Springer Science and Business Media LLC

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s00253-015-6520-6.pdf

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3. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254

4. Chan CH, Wilbanks CC, Makhatadze GI, Wong KB (2012) Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values. PLoS One 7(1):e30296

5. Chen VB, Arendall WB, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC (2010) MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66:12–21

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