Difference between revisions of "Part:BBa K3468019:Experience"
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The thermal stability improvement result was obtained by the evaluation of I-Mutant website, and the thermal stability improvement result of -2.5879 was also obtained by the FoldX evaluation. | The thermal stability improvement result was obtained by the evaluation of I-Mutant website, and the thermal stability improvement result of -2.5879 was also obtained by the FoldX evaluation. | ||
− | [[File:N275F222.png|400px|]] | + | [[File:N275F222.png|400px|thumb|left|Fig.2 N275F in PyMOL]] |
− | [[File:N275F.png|400px|]] | + | [[File:N275F.png|400px|thumb|left|Fig.3 the result of N275F in I-Mutant]] |
References | References |
Revision as of 07:02, 25 October 2020
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Applications of BBa_K3468019
The thermal stability improvement result was obtained by the evaluation of I-Mutant website, and the thermal stability improvement result of -2.5879 was also obtained by the FoldX evaluation.
References
[1]Wang J, Yao L. Dissecting C-H∙∙∙π and N-H∙∙∙π Interactions in Two Proteins Using a Combined Experimental and Computational Approach. Sci Rep. 2019 Dec 27;9(1):20149.
[2]Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R. Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis. Chembiochem. 2018 Jul 16;19(14):1471-1475.
[3]Zhang X, Zhang Y, Yang G, Xie Y, Xu L, An J, Cui L, Feng Y. Modulation of the thermostability and substrate specificity of Candida rugosa lipase1 by altering the acyl-binding residue Gly414 at the α-helix-connecting bend. Enzyme Microb Technol. 2016 Jan;82:34-41.
[4]Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science. 1985 Jul 5;229(4708):23-8.
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