Literature DB >> 19157087

Protein stabilization by the rational design of surface charge-charge interactions.

Katrina L Schweiker1, George I Makhatadze.   

Abstract

The design of proteins with increased stability has many important applications in biotechnology. In recent years, strategies involving directed evolution, sequence-based design, or computational design have proven successful for generating stabilized proteins. A brief overview of the various methods that have been used to increase protein stability is presented, followed by a detailed example of how the rational design of surface charge-charge interactions has provided a robust method for protein stabilization.

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Year:  2009        PMID: 19157087     DOI: 10.1007/978-1-59745-367-7_11

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  16 in total

1.  Increasing protein stability: importance of DeltaC(p) and the denatured state.

Authors:  Hailong Fu; Gerald Grimsley; J Martin Scholtz; C Nick Pace
Journal:  Protein Sci       Date:  2010-05       Impact factor: 6.725

2.  Rational stabilization of enzymes by computational redesign of surface charge-charge interactions.

Authors:  Alexey V Gribenko; Mayank M Patel; Jiajing Liu; Scott A McCallum; Chunyu Wang; George I Makhatadze
Journal:  Proc Natl Acad Sci U S A       Date:  2009-02-05       Impact factor: 11.205

3.  A method to rationally increase protein stability based on the charge-charge interaction, with application to lipase LipK107.

Authors:  Lujia Zhang; Xiaomang Tang; Dongbing Cui; Zhiqiang Yao; Bei Gao; Shuiqin Jiang; Bo Yin; Y Adam Yuan; Dongzhi Wei
Journal:  Protein Sci       Date:  2013-11-22       Impact factor: 6.725

4.  A critical review of five machine learning-based algorithms for predicting protein stability changes upon mutation.

Authors:  Jianwen Fang
Journal:  Brief Bioinform       Date:  2020-07-15       Impact factor: 11.622

5.  The role of surface electrostatics on the stability, function and regulation of human cystathionine β-synthase, a complex multidomain and oligomeric protein.

Authors:  Angel L Pey; Tomas Majtan; Jan P Kraus
Journal:  Biochim Biophys Acta       Date:  2014-04-26

6.  Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model.

Authors:  Ji-Guo Su; Xiao-Ming Han; Shu-Xin Zhao; Yan-Xue Hou; Xing-Yuan Li; Li-Sheng Qi; Ji-Hua Wang
Journal:  J Mol Model       Date:  2016-03-28       Impact factor: 1.810

7.  Increasing sequence diversity with flexible backbone protein design: the complete redesign of a protein hydrophobic core.

Authors:  Grant S Murphy; Jeffrey L Mills; Michael J Miley; Mischa Machius; Thomas Szyperski; Brian Kuhlman
Journal:  Structure       Date:  2012-05-24       Impact factor: 5.006

8.  PROTS: a fragment based protein thermo-stability potential.

Authors:  Yunqi Li; Jian Zhang; David Tai; C Russell Middaugh; Yang Zhang; Jianwen Fang
Journal:  Proteins       Date:  2011-10-05

Review 9.  Thermophilic proteins: insight and perspective from in silico experiments.

Authors:  Fabio Sterpone; Simone Melchionna
Journal:  Chem Soc Rev       Date:  2011-10-05       Impact factor: 54.564

10.  PROTS-RF: a robust model for predicting mutation-induced protein stability changes.

Authors:  Yunqi Li; Jianwen Fang
Journal:  PLoS One       Date:  2012-10-15       Impact factor: 3.240

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