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Methods in Enzymology|January 1, 1986
Study of protein dynamics by X-ray diffractionD Ringe, G A PetskoCurrent Opinion in Chemical Biology|February 19, 2000
Observation of unstable species in enzyme-catalyzed transformations using protein crystallographyG A Petsko, D RingeProtein Engineering|December 1, 1987
The 3.0 A crystal structure of xylose isomerase from Streptomyces olivochromogenesG K Farber, G A Petsko, D RingeBiochemistry|March 17, 1999
Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemaseA A Morollo, G A Petsko, D RingeProtein Engineering|December 1, 1990
The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azideB L Stoddard, D Ringe, G A PetskoBiochemistry|February 11, 1997
Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolutionJ P Shaw, G A Petsko, D RingeNature Structural Biology|January 14, 2000
Solvent mobility and the protein 'glass' transitionD Vitkup, D Ringe, G A Petsko, et al.Biochemistry|August 9, 1994
Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastaseX Ding, B F Rasmussen, G A Petsko, et al.Biochemistry|March 21, 1995
Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complexK N Allen, A Lavie, G A Petsko, et al.Biochemistry|May 10, 1994
X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysisA Lavie, K N Allen, G A Petsko, et al.Pageof 30