Observation of the cascaded atomic-to-global length scales driving protein motion
- *Department of Physics and Astronomy, University of Rochester, Bausch & Lomb Hall, Rochester, NY 14627-0171; and †Departments of Physics and Chemistry, University of Toronto, 60-80 St. George Street, Toronto, ON, Canada M5S 3H6
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Edited by Robin M. Hochstrasser, University of Pennsylvania, Philadelphia, PA, and approved February 11, 2003 (received for review October 25, 2002)
Abstract
Model studies of the ligand photodissociation process of carboxymyoglobin have been conducted by using amplified few-cycle laser pulses short enough in duration (<10 fs) to capture the phase of the induced nuclear motions. The reaction-driven modes are observed directly in real time and depict the pathway by which energy liberated in the localized reaction site is efficiently channeled to functionally relevant mesoscale motions of the protein.
Footnotes
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↵ ‡ To whom correspondence should be addressed. E-mail: rjdmiller{at}lphys.chem.utoronto.ca.
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This paper was submitted directly (Track II) to the PNAS office.
- Abbreviations:
- MbCO,
- carboxymyoglobin;
- deoxyMb,
- deoxymyoglobin;
- cyt c,
- cytochrome c;
- LPSVD,
- linear predictive singular value decomposition;
- IF,
- instantaneous frequency
- Copyright © 2003, The National Academy of Sciences
