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Science 23 March 2001:
Vol. 291. no. 5512, pp. 2329 - 2330
DOI: 10.1126/science.1060383

Perspectives

STRUCTURAL BIOLOGY:
Flipping a Switch

Matthias Buck and Michael K. Rosen

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.).


The authors are in the Howard Hughes Medical Institute and Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA. E-mail: rosen{at}mrnmr1.mskcc.org

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The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain.
T. Shen, C. Zong, D. Hamelberg, J. A. McCammon, and P. G. Wolynes (2005)
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Investigation of the Role of Electrostatic Charge in Activation of the Escherichia coli Response Regulator CheY.
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Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations.
B. Ma, M. Shatsky, H. J. Wolfson, and R. Nussinov (2002)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)