Journal ArticleDOI
Protein disulfide engineering.
TLDR
Progress in disulfide engineering is reviewed, with an emphasis on the issue of stability and computational methods that facilitate engineering efforts.About:
This article is published in FEBS Letters.The article was published on 2014-01-21. It has received 205 citations till now.read more
Citations
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Forces stabilizing proteins
TL;DR: What has been learned about the major forces stabilizing proteins since the late 1980s when site‐directed mutagenesis became possible is summarized.
Journal ArticleDOI
Review: Engineering of thermostable enzymes for industrial applications
TL;DR: The most relevant enzymes that are used for industrial applications are provided and the strategies that are adopted to enhance enzyme stability and/or activity are discussed, along with some of the most relevant achievements.
Journal ArticleDOI
Protein stability: a crystallographer's perspective.
TL;DR: This review will focus on factors affecting protein stability on a somewhat practical level, particularly from the view of a protein crystallographer.
Journal ArticleDOI
Principles of Protein Stability and Their Application in Computational Design
TL;DR: The computational stability design methods have advanced over the past two decades starting from methods that selectively addressed only some aspects of marginal stability, such as thermodynamic, cellular, and evolutionary principles and mechanisms that underlie marginal stability as mentioned in this paper.
Journal ArticleDOI
FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
TL;DR: In this review different algorithms for the prediction of beneficial mutation sites to enhance protein stability are summarized and the advantages and disadvantages of FoldX are highlighted.
References
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Journal ArticleDOI
Model building of disulfide bonds in proteins with known three-dimensional structure.
Bart Hazes,Bauke W. Dijkstra +1 more
TL;DR: As an aid in the selection of sites in a protein where a disulfide bond might be engineered, a computer program has been developed that generates S gamma positions that satisfy the requirement that, with ideal values for the C alpha-C beta and C beta-S gamma bond lengths and for the bond angle at C beta, the distance between S gamma of residue 1 and C Beta of residue 2 in a pair is at, or very close to its ideal value.
Journal ArticleDOI
Disulfide bonds and thermal stability in T4 lysozyme
TL;DR: Thermodynamic data presented here demonstrate that an engineered 3-97 disulfide bond previously shown to stabilize T4 lysozyme in vitro against irreversible thermal inactivation also stabilizes the molecule against reversible thermal unfolding, and suggest that the 3- 97 disulfides provides stability to irreversible inactivation primarily via a pathway that is independent of its thermodynamic contribution.
Journal ArticleDOI
Molecular dynamics simulations as a tool for improving protein stability
TL;DR: The results show that MD simulations are capable of identifying mobile protein domains that can successfully be used as a target for stability enhancement by the introduction of a disulfide cross-link.
Journal ArticleDOI
Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB
Markus A. Seeger,Christoph von Ballmoos,Thomas Eicher,Lorenz Brandstätter,François Verrey,Kay Diederichs,Klaas M. Pos +6 more
TL;DR: The results support the presence of the asymmetric AcrB trimer in E. coli membranes and the functional rotation mechanism.
Journal ArticleDOI
An engineered intersubunit disulfide enhances the stability and DNA binding of the N-terminal domain of lambda repressor.
Robert T. Sauer,Kathleen Hehir,Robert Stearman,Michael A. Weiss,Michael A. Weiss,Anna Jeitler-Nilsson,E. G. Suchanek,Carl O. Pabo +7 more
TL;DR: It is found that the Cys-88 protein forms a disulfide-bonded dimer that is very stable to reduction by dithiothreitol and has increased operator DNA binding activity and covalent Cys88-Cys88' dimer is considerably more stable than the wild-type protein to thermal denaturation or urea denaturation.