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
More filters
Journal ArticleDOI
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
More filters
Journal ArticleDOI
Probing protein structure by limited proteolysis.
Angelo Fontana,Patrizia Polverino de Laureto,Barbara Spolaore,Erica Frare,Paola Picotti,Marcello Zambonin +5 more
TL;DR: The results underscore the utility of the limited proteolysis approach for unravelling molecular features of proteins and appear to prompt its systematic use as a simple first step in the elucidation of structure-dynamics-function relationships of a novel and rare protein, especially if available in minute amounts.
Journal ArticleDOI
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds.
TL;DR: It is quite remarkable that RNase T1 can fold and function with both disulfide bonds broken and the cysteine residues carboxymethylated and a new equation for predicting the effect of a cross-link on the conformational entropy of a protein is proposed.
Journal ArticleDOI
Disulfide bonds and the stability of globular proteins.
TL;DR: Experimental thermodynamic evidence is examined and it is confirmed that enthalpic and native‐state effects are often significant and lend support to any of the current theories regarding the stabilization of proteins by disulfide bonds.
Journal ArticleDOI
Substantial increase of protein stability by multiple disulphide bonds.
TL;DR: It is demonstrated that a combination of disulphide bonds, each of which contributes to stability, can achieve substantial overall improvement in the stability of a protein.