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Molecular chaperones in cellular protein folding
Author(s) -
Martin Jörg,
Hartl F.Ulrich
Publication year - 1994
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.950160916
Subject(s) - protein folding , co chaperone , folding (dsp implementation) , chemical chaperone , computational biology , function (biology) , chemistry , chaperone (clinical) , biology , biochemistry , microbiology and biotechnology , hsp90 , unfolded protein response , heat shock protein , medicine , gene , pathology , electrical engineering , engineering
The discovery of “molecular chaperones” has dramatically changed our concept of cellular protein folding. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformation in a reaction mediated by these versatile helper proteins. Understanding the structure and function of molecular chaperones is likely to yield useful applications for medicine and biotechnology in the future.