Data Entry: Please note that the research database will be replaced by UNIverse by the end of October 2023. Please enter your data into the system https://universe-intern.unibas.ch. Thanks
Molecular chaperones and their denaturing effect on client proteins
Journal
Journal of Biomolecular NMR
Volume
75
Number
1
Pages / Article-Number
1-8
Keywords
Chaotropic denaturants; Molecular chaperones; NMR spectroscopy; Protein folding; Protein stability; Protein structure; Proteins dynamics; Thermal unfolding
Mesh terms
Humans; Models, Molecular; Molecular Chaperones, chemistry; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Protein Unfolding; Proteins, chemistry; Solubility; Structure-Activity Relationship
Abstract
Advanced NMR methods combined with biophysical techniques have recently provided unprecedented insight into structure and dynamics of molecular chaperones and their interaction with client proteins. These studies showed that several molecular chaperones are able to dissolve aggregation-prone polypeptides in aqueous solution. Furthermore, chaperone-bound clients often feature fluid-like backbone dynamics and chaperones have a denaturing effect on clients. Interestingly, these effects that chaperones have on client proteins resemble the effects of known chaotropic substances. Following this analogy, chaotropicity could be a fruitful concept to describe, quantify and rationalize molecular chaperone function. In addition, the observations raise the possibility that at least some molecular chaperones might share functional similarities with chaotropes. We discuss these concepts and outline future research in this direction.
