Premium
Chaperone discovery
Author(s) -
Quan Shu,
Bardwell James C. A.
Publication year - 2012
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201200059
Subject(s) - chaperone (clinical) , protein folding , co chaperone , computational biology , biology , chemistry , microbiology and biotechnology , biochemistry , hsp90 , heat shock protein , gene , medicine , pathology
Molecular chaperones assist de novo protein folding and facilitate the refolding of stress‐denatured proteins. The molecular chaperone concept was coined nearly 35 years ago, and since then, tremendous strides have been made in understanding how these factors support protein folding. Here, we focus on how various chaperone proteins were first identified to play roles in protein folding. Examples are used to illustrate traditional routes of chaperone discovery and point out their advantages and limitations. Recent advances, including the development of folding biosensors and promising methods for the stabilization of proteins in vivo, provide new routes for chaperone discovery.