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Biophysical Journal 65: 1660-1665 (1993)
© 1993 the Biophysical Society

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A photoacoustic calorimetry study of horse carboxymyoglobin on the 10-nanosecond time scale.

C L Norris and K S Peters

Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.

ABSTRACT

The development of a photoacoustic calorimeter with a time resolution of 10 ns is presented, and the dynamics of the enthalpy and volume changes found in the photodissociation of CO from horse carboxymyoglobin are examined. With this enhanced time resolution a new transient species, the lifetime of which is 29 ns at 20 degrees C, is observed in the ligand dissociation process.




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Proc. Natl. Acad. Sci. USAHome page
G. Dadusc, J. P. Ogilvie, P. Schulenberg, U. Marvet, and R. J. D. Miller
Diffractive optics-based heterodyne-detected four-wave mixing signals of protein motion: From "protein quakes" to ligand escape for myoglobin
PNAS, May 3, 2001; (2001) 101130298.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
G. Dadusc, J. P. Ogilvie, P. Schulenberg, U. Marvet, and R. J. D. Miller
Diffractive optics-based heterodyne-detected four-wave mixing signals of protein motion: From "protein quakes" to ligand escape for myoglobin
PNAS, May 22, 2001; 98(11): 6110 - 6115.
[Abstract] [Full Text] [PDF]




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Copyright © 1993 by the Biophysical Society.