Glycine Substitution of Residues with Unfavored Dihedral Angles Improves Protein Thermostability

Glycine Substitution of Residues with Unfavored Dihedral Angles Improves Protein Thermostability

Single mutations that can substantially enhance stability are highly desirable for protein engineering. However, it is generally rare for this kind of mutant to emerge from directed evolution experiments. This study used computational approaches to identify hotspots in a diacylglycerol-specific lipa...

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Bibliographic Details
Main Authors: Zhili Lu, Qiaoxian Zhong, Jingxian Li, Bingjie Zhou, Yan-Ni Xing, Kaien Liu, Kexin Cao, Dongming Lan, Teng Zhou, Yonghua Wang, Jiaqi Wang
Format: Article
Language:English
Published: MDPI AG 2022-08-01
Series:Catalysts
Subjects:
protein thermostability
lipase
structure-guided rational design
glycine substitution
dihedral angle
Ramachandran plot
Online Access:https://www.mdpi.com/2073-4344/12/8/898

Internet

https://www.mdpi.com/2073-4344/12/8/898

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