Title : Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

Pub. Date : 1994 Mar 17

PMID : 7908413






2 Functional Relationships(s)
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1 Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin. Amides GroEL Escherichia coli
2 Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin. Amides GroEL Escherichia coli