Article
Hydrogen exchange reveals a stable and expandable core within the aspartate receptor cytoplasmic domain.
The Journal of biological chemistry - 16 Nov 2001
Murphy O J, Yi X, Weis R M, Thompson L K
Abstract excerpt
Intensive study of bacterial chemoreceptors has not yet revealed how receptor methylation and ligand binding alter the interactions between the receptor cytoplasmic domain and the CheA kinase to control kinase activity. Both monomeric and dimeric forms of an Asp receptor cytoplasmic fragment have been shown to be highly dynamic, with a small core of slowly exchanging amide hydrogens (Seeley, S. K., Weis, R. M.,...
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