Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM035940-12
Application #
2178148
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1986-01-01
Project End
1999-02-28
Budget Start
1996-03-01
Budget End
1997-02-28
Support Year
12
Fiscal Year
1996
Total Cost
Indirect Cost
Name
State University of New York at Buffalo
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
038633251
City
Buffalo
State
NY
Country
United States
Zip Code
14260
Caro, José A; Wand, A Joshua (2018) Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology. Methods 148:67-80
Liu, Weixia; Rumbley, Jon N; Englander, S Walter et al. (2009) Fast structural dynamics in reduced and oxidized cytochrome c. Protein Sci 18:670-4
Gledhill Jr, John M; Joshua Wand, A (2008) Optimized angle selection for radial sampled NMR experiments. J Magn Reson 195:169-78
Bedard, Sabrina; Mayne, Leland C; Peterson, Ronald W et al. (2008) The foldon substructure of staphylococcal nuclease. J Mol Biol 376:1142-54
Calhoun, Jennifer R; Liu, Weixia; Spiegel, Katrin et al. (2008) Solution NMR structure of a designed metalloprotein and complementary molecular dynamics refinement. Structure 16:210-5
Gledhill, John M; Wand, A Joshua (2007) Phasing arbitrarily sampled multidimensional NMR data. J Magn Reson 187:363-70
Pometun, Maxim S; Peterson, Ronald W; Babu, Charles R et al. (2006) Cold denaturation of encapsulated ubiquitin. J Am Chem Soc 128:10652-3
Koder, Ronald L; Valentine, Kathleen G; Cerda, Jose et al. (2006) Nativelike structure in designed four alpha-helix bundles driven by buried polar interactions. J Am Chem Soc 128:14450-1
Whitten, Steven T; Kurtz, Andrew J; Pometun, Maxim S et al. (2006) Revealing the nature of the native state ensemble through cold denaturation. Biochemistry 45:10163-74
Valentine, Kathleen G; Pometun, Maxim S; Kielec, Joseph M et al. (2006) Magnetic susceptibility-induced alignment of proteins in reverse micelles. J Am Chem Soc 128:15930-1

Showing the most recent 10 out of 53 publications