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Corey W. Meadows, Ph.D.

Affiliations: 
2014 Chemistry University of California, Berkeley, Berkeley, CA, United States 
Area:
fundamental aspects of enzyme catalysis
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"Corey Meadows"
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Judith Pollock Klinman grad student 2014 UC Berkeley
 (Analysis of Fluorescence Dynamics Within a Thermophilic Alcohol Dehydrogenase.)

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Meadows CW, Balakrishnan G, Kier BL, et al. (2015) Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase. Journal of the American Chemical Society
Meadows CW, Tsang JE, Klinman JP. (2014) Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication. Journal of the American Chemical Society. 136: 14821-33
Meadows CW, Ou R, Klinman JP. (2014) Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis. The Journal of Physical Chemistry. B. 118: 6049-61
Meadows CW, Ou R, Klinman JP. (2014) Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: Relationship of temperature-dependent changes in fluorescence to catalysis Journal of Physical Chemistry B. 118: 6049-6061
Meadows CW, Tsang JE, Klinman JP. (2014) Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication Journal of the American Chemical Society. 136: 14821-14833
Meadows CW, Klinman JP. (2014) Modulation of Active Site Picosecond Dynamics in Mutant Forms of a Thermophilic Alcohol Dehydrogenase (HT-ADH) Biophysical Journal. 106: 648a
Nagel ZD, Meadows CW, Dong M, et al. (2012) Active site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures Biochemistry. 51: 4147-4156
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