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Journal of Molecular Biology|May 20, 1994
Analysis of two-residue turns in proteinsC Mattos, G A Petsko, M KarplusNature Structural Biology|March 1, 1997
A comparison between molecular dynamics and X-ray results for dissociated CO in myoglobinD Vitkup, G A Petsko, M KarplusScience (New York, N.Y.)|September 21, 1990
Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loopD Joseph, G A Petsko, M KarplusProteins|January 1, 1987
Estimation of uncertainties in X-ray refinement results by use of perturbed structuresJ Kuriyan, M Karplus, G A PetskoProtein Engineering|November 1, 1995
Use of a minimum perturbation approach to predict TIM mutant structuresD Joseph-McCarthy, G A Petsko, M KarplusJournal of Molecular Biology|November 5, 1986
X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolutionJ Kuriyan, S Wilz, M Karplus, et al.Nature Structural Biology|January 14, 2000
Solvent mobility and the protein 'glass' transitionD Vitkup, D Ringe, G A Petsko, et al.Journal of Molecular Biology|July 20, 1986
Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation by molecular dynamicsJ Kuriyan, G A Petsko, R M Levy, et al.Biochemistry|June 18, 1991
Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathwayR C Davenport, P A Bash, B A Seaton, et al.Pageof 39