Kim A. Sharp
Affiliations: | University of Pennsylvania, Philadelphia, PA, United States |
Area:
General Biophysics, Biochemistry, Physical ChemistryGoogle:
"Kim Sharp"Mean distance: (not calculated yet)
Children
Sign in to add traineeKelly R. Gallagher | grad student | 1994-2002 | Penn (Chemistry Tree) |
Ryan G. Coleman | grad student | 2009 | Penn |
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Publications
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Fuglestad B, Gupta K, Wand AJ, et al. (2019) Water loading driven size, shape, and composition of cetyltrimethylammonium/hexanol/pentane reverse micelles. Journal of Colloid and Interface Science. 540: 207-217 |
Sharp KA. (2019) Companion Simulations and Modeling to NMR-Based Dynamical Studies of Proteins. Methods in Enzymology. 615: 1-41 |
Wand AJ, Sharp KA. (2018) Measuring Entropy in Molecular Recognition by Proteins. Annual Review of Biophysics |
Caro JA, Harpole KW, Kasinath V, et al. (2017) Entropy in molecular recognition by proteins. Proceedings of the National Academy of Sciences of the United States of America |
O'Brien ES, Wand AJ, Sharp KA. (2016) On the ability of molecular dynamics force fields to recapitulate NMR derived protein side chain NMR order parameters. Protein Science : a Publication of the Protein Society |
Sharp KA. (2016) Unpacking the origins of in-cell crowding. Proceedings of the National Academy of Sciences of the United States of America. 113: 1684-5 |
Fuglestad B, Gupta K, Wand AJ, et al. (2016) Characterization of Cetyl Trimethylammonium Bromide/Hexanol Reverse Micelles by Experimentally Benchmarked Molecular Dynamics Simulations. Langmuir : the Acs Journal of Surfaces and Colloids |
Sharp KA. (2015) Analysis of the size dependence of macromolecular crowding shows that smaller is better. Proceedings of the National Academy of Sciences of the United States of America. 112: 7990-5 |
Sharp KA, O'Brien E, Kasinath V, et al. (2015) On the relationship between NMR-derived amide order parameters and protein backbone entropy changes. Proteins. 83: 922-30 |
Kasinath V, Fu Y, Sharp KA, et al. (2015) A sharp thermal transition of fast aromatic-ring dynamics in ubiquitin. Angewandte Chemie (International Ed. in English). 54: 102-7 |