Flipping a Switch
- 23 March 2001
- journal article
- editorial
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 291 (5512) , 2329-2330
- https://doi.org/10.1126/science.1060383
Abstract
Proteins are not inert structures but are constantly in motion. In their Perspective, Buck and Rosen describe new experiments that use the power of nuclear magnetic resonance to correlate motions in nitrogen regulatory protein C, a bacterial signaling protein, with its biological activity ( Volkman et al.).Keywords
This publication has 12 references indexed in Scilit:
- Two-State Allosteric Behavior in a Single-Domain Signaling ProteinScience, 2001
- Analyzing protein functions in four dimensionsNature Structural & Molecular Biology, 2000
- Structure of a transiently phosphorylated switch in bacterial signal transductionNature, 1999
- Structural dynamics in the C-terminal domain of calmodulin at low calcium levels 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0FNature, 1999
- A Trivalent System from Vancomycin· d -Ala- d -Ala with Higher Affinity Than Avidin·BiotinScience, 1998
- Probing molecular motion by NMRCurrent Opinion in Structural Biology, 1997
- Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surfaceJournal of Molecular Biology, 1997
- A perspective on biological catalysisNature Structural & Molecular Biology, 1996
- Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C,15N) NMR SpectroscopyBiochemistry, 1994