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Journal of Molecular Biology|August 5, 1983
Refined crystal structure of carboxypeptidase A at 1.54 A resolutionD C Rees, M Lewis, W N LipscombProceedings of the National Academy of Sciences of the United States of America|July 1, 1975
Molecular orbital studies of enzyme activity: I: Charge relay system and tetrahedral intermediate in acylation of serine proteinasesS Scheiner, D A Kleier, W N LipscombActa Crystallographica. Section D, Biological Crystallography|October 3, 1998
Detection and use of pseudo-translation in determination of protein structuresY M Chook, W N Lipscomb, H KeProceedings of the National Academy of Sciences of the United States of America|November 30, 2000
Coevolution of transcriptional and allosteric regulation at the chorismate metabolic branch point of Saccharomyces cerevisiaeS Krappmann, W N Lipscomb, G H BrausProceedings of the National Academy of Sciences of the United States of America|September 15, 1993
Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analogY M Chook, H Ke, W N LipscombJournal of Molecular Biology|April 5, 1993
Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatinH Kim, S K Burley, W N LipscombBiochemistry|April 24, 1990
Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylaseJ W Stebbins, Y Zhang, E R KantrowitzThe Journal of Biological Chemistry|January 25, 1988
Site-directed mutagenesis of a residue located in the regulatory site of Escherichia coli aspartate transcarbamoylase. Involvement of lysine 94 in effector binding and the allosteric mechanismY Zhang, M M Ladjimi, E R KantrowitzBiochemistry|March 3, 1999
Rate-determining step of Escherichia coli alkaline phosphatase altered by the removal of a positive charge at the active centerL Sun, D C Martin, E R KantrowitzThe Journal of Biological Chemistry|February 21, 1997
Importance of the dimer-dimer interface for allosteric signal transduction and AMP cooperativity of pig kidney fructose-1,6-bisphosphatase. Site-specific mutagenesis studies of Glu-192 and Asp-187 residues on the 190's loopG Lu, E L Giroux, E R KantrowitzPageof 22