David Robert Shortle, M.D., Ph.D.
|1984-||Biological Chemistry||Johns Hopkins University, Baltimore, MD|
Area:General Biophysics, Biochemistry
Google:"David Robert Shortle, M.D., Ph.D."
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|Shortle D. (2009) One sequence plus one mutation equals two folds. Proceedings of the National Academy of Sciences of the United States of America. 106: 21011-2|
|Gebel EB, Shortle D. (2007) Characterization of denatured proteins using residual dipolar couplings. Methods in Molecular Biology (Clifton, N.J.). 350: 39-48|
|Ohnishi S, Kamikubo H, Onitsuka M, et al. (2006) Conformational preference of polyglycine in solution to elongated structure. Journal of the American Chemical Society. 128: 16338-44|
|Gebel EB, Ruan K, Tolman JR, et al. (2006) Multiple alignment tensors from a denatured protein. Journal of the American Chemical Society. 128: 9310-1|
|Fang Q, Shortle D. (2006) Protein refolding in silico with atom-based statistical potentials and conformational search using a simple genetic algorithm. Journal of Molecular Biology. 359: 1456-67|
|Fang Q, Shortle D. (2005) Enhanced sampling near the native conformation using statistical potentials for local side-chain and backbone interactions. Proteins. 60: 97-102|
|Fang Q, Shortle D. (2005) A consistent set of statistical potentials for quantifying local side-chain and backbone interactions. Proteins. 60: 90-6|
|Ohnishi S, Lee AL, Edgell MH, et al. (2004) Direct demonstration of structural similarity between native and denatured eglin C. Biochemistry. 43: 4064-70|
|Fang Q, Shortle D. (2003) Prediction of protein structure by emphasizing local side-chain/backbone interactions in ensembles of turn fragments. Proteins. 53: 486-90|
|Ohnishi S, Shortle D. (2003) Effects of denaturants and substitutions of hydrophobic residues on backbone dynamics of denatured staphylococcal nuclease. Protein Science : a Publication of the Protein Society. 12: 1530-7|