| Literature DB >> 31432502 |
Damien Hall1,2.
Abstract
The holdase paradigm of chaperone action involves preferential binding by the chaperone to the unfolded protein state, thereby preventing it from either, associating with other unstable proteins (to form large dysfunctional aggregates), or being degraded by the proteolytic machinery of the cell/organism. In this paper, we examine the necessary physical constraints imposed upon the holdase chaperone response in a cell-like environment and use these limitations to comment on the likely nature of the optimal form of chaperone response in vivo. Published 2019. This article is a U.S. Government work and is in the public domain in the USA.Entities:
Keywords: biophysical modelling; holdase; molecular chaperones; protein folding; small heat shock proteins
Mesh:
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Year: 2019 PMID: 31432502 PMCID: PMC6961976 DOI: 10.1002/1873-3468.13580
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 3.864