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Protein 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|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 PetskoProteins|September 19, 1997
Use of the multiple copy simultaneous search (MCSS) method to design a new class of picornavirus capsid binding drugsD Joseph-McCarthy, J M Hogle, 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.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.Pageof 40