Covalent Structural Changes in Unfolded GroES That Lead to Amyloid Fibril Formation Detected by NMR: INSIGHT INTO INTRINSICALLY DISORDERED PROTEINS

Co-chaperonin GroES from Escherichia coli works with chaperonin GroEL to mediate the folding reactions of various proteins. However, under specific conditions, i.e. the completely disordered state in guanidine hydrochloride, this molecular chaperone forms amyloid fibrils similar to those observed in...

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Hlavní autoři: Iwasa, Hisanori, Meshitsuka, Shunsuke, Hongo, Kunihiro, Mizobata, Tomohiro, Kawata, Yasushi
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2011
Témata:
Glycobiology and Extracellular Matrices
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3122234/
https://ncbi.nlm.nih.gov/pubmed/21507961
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.228445
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