Literature DB >> 31432502

On the nature of the optimal form of the holdase-type chaperone stress response.

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:

Substances:

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


  122 in total

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