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Science 1 March 1991:
Vol. 251. no. 4997, pp. 1051 - 1054
DOI: 10.1126/science.1998121
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Articles

Science, Vol 251, Issue 4997, 1051-1054
Copyright © 1991 by American Association for the Advancement of Science

articles

Direct observation of global protein motion in hemoglobin and myoglobin on picosecond time scales

L Genberg, L Richard, G McLendon, and RJ Miller

Department of Chemistry, University of Rochester, NY 14627.

Picosecond phase-grating spectroscopy is highly sensitive to density changes and provides a new holographic approach to the study of protein dynamics. Photodissociation of carbon monoxide from heme proteins induces a well-defined transition from a ligated to a deoxy structure that is important to hemoglobin and myoglobin functionality. Grating spectroscopy was used to observe protein-driven density waves on a picosecond time scale after carbon monoxide dissociation. This result demonstrates that global tertiary structure changes of proteins occur on an extremely fast time scale and provides new insight into the biomechanics of deterministic protein motion.


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