Eric D. Watt, Ph.D.

Affiliations: 
Yale University, New Haven, CT 
Area:
dynamic and structural properties of proteins
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"Eric Watt"
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J. Patrick Loria grad student 2012 Yale
 (The mechanism and modulation of rate-limiting millisecond enzyme motions in ribonuclease A.)
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Publications

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Kleinstreuer NC, Ceger P, Watt ED, et al. (2016) Development and Validation of a Computational Model for Androgen Receptor Activity. Chemical Research in Toxicology
Nuzzio KM, Watt ED, Boettcher JM, et al. (2016) High-Resolution NMR Studies of Human Tissue Factor. Plos One. 11: e0163206
Courtney JM, Ye Q, Nesbitt AE, et al. (2015) Experimental Protein Structure Verification by Scoring with a Single, Unassigned NMR Spectrum. Structure (London, England : 1993)
Watt ED, Rienstra CM. (2014) Recent advances in solid-state nuclear magnetic resonance techniques to quantify biomolecular dynamics. Analytical Chemistry. 86: 58-64
Watt ED, Rivalta I, Whittier SK, et al. (2011) Reengineering rate-limiting, millisecond enzyme motions by introduction of an unnatural amino acid. Biophysical Journal. 101: 411-20
Doucet N, Watt ED, Loria JP. (2009) The flexibility of a distant loop modulates active site motion and product release in ribonuclease A. Biochemistry. 48: 7160-8
Dethoff EA, Hansen AL, Musselman C, et al. (2008) Characterizing complex dynamics in the transactivation response element apical loop and motional correlations with the bulge by NMR, molecular dynamics, and mutagenesis. Biophysical Journal. 95: 3906-15
Croke RL, Sallum CO, Watson E, et al. (2008) Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli. Protein Science : a Publication of the Protein Society. 17: 1434-45
Loria JP, Berlow RB, Watt ED. (2008) Characterization of enzyme motions by solution NMR relaxation dispersion. Accounts of Chemical Research. 41: 214-21
Watt ED, Shimada H, Kovrigin EL, et al. (2007) The mechanism of rate-limiting motions in enzyme function. Proceedings of the National Academy of Sciences of the United States of America. 104: 11981-6
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