Intrinsic dynamics of an enzyme underlies catalysis

Elan Z. Eisenmesser, Oscar Millet, Wladimir Labeikovsky, Dmitry M. Korzhnev, Magnus Wolf-Watz, Daryl A. Bosco, Jack J. Skalicky, Lewis E. Kay and Dorothee Kern ()
Additional contact information
Elan Z. Eisenmesser: Brandeis University
Oscar Millet: University of Toronto
Wladimir Labeikovsky: Brandeis University
Dmitry M. Korzhnev: University of Toronto
Magnus Wolf-Watz: Brandeis University
Daryl A. Bosco: Brandeis University
Jack J. Skalicky: National High Magnetic Field Laboratory at Florida State University
Lewis E. Kay: University of Toronto
Dorothee Kern: Brandeis University

Nature, 2005, vol. 438, issue 7064, 117-121

Abstract: Split personality Here's a new way to look at familiar enzymes. A new technology that can detect ultra-rare states of a protein (cyclophilin A in this instance) shows that rather than having a range of conformations to which it resorts during catalysis, it has them all before it starts. Protein motions needed for catalysis are intrinsic to the enzyme and take in the whole molecule, not just the traditional centre of attention, the active site.

Date: 2005
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DOI: 10.1038/nature04105

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