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G A Petsko

Showing results (91-100 of 192) with videos related to

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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.
Biochemical Society Transactions|April 1, 1984
Probing the catalytic mechanism of yeast triose phosphate isomerase by site-specific mutagenesisG A Petsko, R C Davenport, D Frankel, 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.
Nature Structural Biology|January 1, 1994
Analogous inhibitors of elastase do not always bind analogouslyC Mattos, B Rasmussen, X Ding, et al.
Biochemistry|April 16, 1991
Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 2. Structural basis of hapten binding and idiotypyR K Strong, G A Petsko, J Sharon, 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.
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.
Pageof 20

Showing results (91-100 of 192) with videos related to

Sort By:
Pageof 20
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.
Biochemical Society Transactions|April 1, 1984
Probing the catalytic mechanism of yeast triose phosphate isomerase by site-specific mutagenesisG A Petsko, R C Davenport, D Frankel, 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.
Nature Structural Biology|January 1, 1994
Analogous inhibitors of elastase do not always bind analogouslyC Mattos, B Rasmussen, X Ding, et al.
Biochemistry|April 16, 1991
Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 2. Structural basis of hapten binding and idiotypyR K Strong, G A Petsko, J Sharon, 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.
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.
Pageof 20