Article
Two-state allosteric behavior in a single-domain signaling protein.
Science (New York, N.Y.) - 23 Mar 2001
Volkman B F, Lipson D, Wemmer D E, Kern D
Abstract excerpt
Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a...
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