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Current Opinion in Structural Biology|December 26, 2001
Proteins in organic solventsC Mattos, D RingeBiochemistry|February 11, 1997
Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolutionJ P Shaw, G A Petsko, D RingeJournal of Molecular Biology|May 20, 1994
Analysis of two-residue turns in proteinsC Mattos, G A Petsko, M KarplusNature Structural Biology|January 14, 2000
Solvent mobility and the protein 'glass' transitionD Vitkup, D Ringe, 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.Proceedings of the National Academy of Sciences of the United States of America|July 1, 1983
Structure of iron superoxide dismutase from Pseudomonas ovalis at 2.9-A resolutionD Ringe, G A Petsko, F Yamakura, et al.Nature|June 4, 1992
Crystalline ribonuclease A loses function below the dynamical transition at 220 KB F Rasmussen, A M Stock, D Ringe, et al.Protein Engineering|March 10, 2000
The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferaseC J Jeffery, L M Gloss, G A Petsko, et al.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.Pageof 221