Assisted Protein Folding by Amphiphiles and Molecular Chaperones
作者： Paul M. Horowitz
DOI: 10.1016/S1569-2558(08)60484-1
关键词:
摘要: Publisher Summary This chapter discusses the folding of soluble globular proteins as assisted by called “chaperonins,” which can operate in vivo and vitro , “amphiphiles” such detergents that appear to share some mechanistic similarities with chaperonins provide both basic practical understanding assistance. The focuses on for aggregation and/or association are major side paths compete folding. studies enzyme rhodanese (EC 2.8.1.1), usefulness a model, issues related chaperonin-assisted Cellular protein disulfide isomerase prolyl have been identified catalysts processes influence proteins. sequence native spontaneously adopts narrow distribution conformational states associated originally folded protein.
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