title: Chaperone discovery.
abstract: 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.
authors.affiliation: Department of Molecular, Cellular, and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI, USA. shuquan@umich.edu
authors.forename: Shu
authors.initials: S
authors.lastname: Quan
authors.forename: James C A
authors.initials: JC
authors.lastname: Bardwell
mesh_terms: D000818:Animals; D001671:Biochemistry; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D006360:Heat-Shock Proteins; D018832:Molecular Chaperones