Structural and thermodynamic analyses of Escherichia coli RNase HI variant with quintuple thermostabilizing mutations
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2007.06104.x/fullpdf
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3. Substantial increase of protein stability by multiple disulphide bonds;Matsumura;Nature,1989
4. Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability;Serrano;J Mol Biol,1993
5. High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation;Akasako;Biochemistry,1995
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