Premium
Mechanisms of Protein Folding: Molecular Chaperones and Their Application in Biotechnology
Author(s) -
Mogk Axel,
Mayer Matthias P.,
Deuerling Elke
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020902)3:9<807::aid-cbic807>3.0.co;2-a
Subject(s) - protein folding , co chaperone , chemical chaperone , computational biology , recombinant dna , chaperone (clinical) , protein engineering , folding (dsp implementation) , bacterial protein , biology , boosting (machine learning) , structural biology , synthetic biology , microbiology and biotechnology , chemistry , biochemistry , gene , hsp90 , heat shock protein , computer science , unfolded protein response , engineering , medicine , electrical engineering , enzyme , machine learning , pathology
To fold or not to fold! Molecular chaperones are highly versatile molecules assisting a large variety of protein folding events during the entire lifespan of proteins. Knowledge about the network and functions of bacterial chaperones offers new prospects to improve the yield of properly folded recombinant proteins, perhaps boosting biotechnology.