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Biochemistry|February 19, 1991
Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferaseA T Danishefsky, J J Onnufer, G A Petsko, et al.Proceedings of the Royal Society of London. Series B, Biological Sciences|April 22, 1983
The iron content of iron superoxide dismutase: determination by anomalous scatteringD Ringe, G A Petsko, F Yamakura, et al.Biochemistry|March 15, 1994
Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active siteD Joseph-McCarthy, E Lolis, E A Komives, et al.Ciba Foundation Symposium|January 1, 1983
The role of mobility in the substrate binding and catalytic machinery of enzymesT Alber, W A Gilbert, D R Ponzi, et al.Biochemistry|September 25, 1990
The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalisB L Stoddard, P L Howell, D Ringe, et al.Journal of Medicinal Chemistry|July 23, 1993
Multiple copy simultaneous search and construction of ligands in binding sites: application to inhibitors of HIV-1 aspartic proteinaseA Caflisch, A Miranker, M KarplusJournal of Molecular Biology|August 25, 1984
An analysis of incorrectly folded protein models. Implications for structure predictionsJ Novotný, R Bruccoleri, M KarplusBiochemistry|May 11, 1982
Protein dynamics in solution and in a crystalline environment: a molecular dynamics studyW F van Gunsteren, M KarplusJournal of Computer-Aided Molecular Design|May 6, 2004
Protein-ligand binding free energy estimation using molecular mechanics and continuum electrostatics. Application to HIV-1 protease inhibitorsV Zoete, O Michielin, M KarplusJournal of Molecular Biology|January 26, 1999
Native proteins are surface-molten solids: application of the Lindemann criterion for the solid versus liquid stateY Zhou, D Vitkup, M KarplusPageof 39