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W N Lipscomb

Showing results (71-80 of 120) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|August 2, 2001
Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanismH Guo, Q Cui, W N Lipscomb, et al.
Biochemistry|August 21, 1990
Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolutionR C Stevens, J E Gouaux, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|October 1, 1972
Similarities between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solutionF A Quiocho, C H McMurray, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1980
Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogueD C Rees, R B Honzatko, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|August 5, 1997
A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditionsG Schnappauf, N Sträter, W N Lipscomb, et al.
Journal of Molecular Biology|December 16, 1994
Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphataseY Zhang, J Y Liang, S Huang, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 29, 1999
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidaseN Sträter, L Sun, E R Kantrowitz, et al.
Proteins|January 29, 2000
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 AL Jin, B Stec, W N Lipscomb, et al.
The Journal of Biological Chemistry|May 25, 1975
Isolation and properties of a species produced by the partial dissociation of aspartate transcarbamylase from Escherichia coliD R Evans, S C Pastra-Landis, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|March 15, 1993
Allosteric transition of fructose-1,6-bisphosphataseJ Y Liang, Y Zhang, S Huang, et al.
Pageof 12

Showing results (71-80 of 120) with videos related to

Sort By:
Pageof 12
Proceedings of the National Academy of Sciences of the United States of America|August 2, 2001
Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanismH Guo, Q Cui, W N Lipscomb, et al.
Biochemistry|August 21, 1990
Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolutionR C Stevens, J E Gouaux, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|October 1, 1972
Similarities between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solutionF A Quiocho, C H McMurray, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1980
Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogueD C Rees, R B Honzatko, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|August 5, 1997
A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditionsG Schnappauf, N Sträter, W N Lipscomb, et al.
Journal of Molecular Biology|December 16, 1994
Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphataseY Zhang, J Y Liang, S Huang, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 29, 1999
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidaseN Sträter, L Sun, E R Kantrowitz, et al.
Proteins|January 29, 2000
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 AL Jin, B Stec, W N Lipscomb, et al.
The Journal of Biological Chemistry|May 25, 1975
Isolation and properties of a species produced by the partial dissociation of aspartate transcarbamylase from Escherichia coliD R Evans, S C Pastra-Landis, W N Lipscomb
Proceedings of the National Academy of Sciences of the United States of America|March 15, 1993
Allosteric transition of fructose-1,6-bisphosphataseJ Y Liang, Y Zhang, S Huang, et al.
Pageof 12