Structure and function in GroEL-mediated protein folding
PB Sigler, Z Xu, HS Rye, SG Burston… - Annual review of …, 1998 - annualreviews.org
Recent structural and biochemical investigations have come together to allow a better
understanding of the mechanism of chaperonin (GroEL, Hsp60)–mediated protein folding,
the final step in the accurate expression of genetic information. Major, asymmetric
conformational changes in the GroEL double toroid accompany binding of ATP and the
cochaperonin GroES. When a nonnative polypeptide, bound to one of the GroEL rings, is
encapsulated by GroES to form a cis ternary complex, these changes drive the polypeptide …
understanding of the mechanism of chaperonin (GroEL, Hsp60)–mediated protein folding,
the final step in the accurate expression of genetic information. Major, asymmetric
conformational changes in the GroEL double toroid accompany binding of ATP and the
cochaperonin GroES. When a nonnative polypeptide, bound to one of the GroEL rings, is
encapsulated by GroES to form a cis ternary complex, these changes drive the polypeptide …
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