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Protein Engineering|April 1, 1991
Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesisR C Stevens, Y M Chook, C Y Cho, et al.Protein Science : a Publication of the Protein Society|November 1, 1992
Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic studyJ W Stebbins, D E Robertson, M F Roberts, et al.Annals of the New York Academy of Sciences|January 1, 1981
A survey of x-ray diffraction studies of enzyme-other molecule interactions as possible models for receptor sitesW N LipscombProceedings of the National Academy of Sciences of the United States of America|July 1, 1980
Carboxypeptidase A mechanismsW N LipscombProceedings of the National Academy of Sciences of the United States of America|December 1, 1973
Enzymatic activities of carobxypeptidase A's in solution and in crystalsW N LipscombCiba Foundation Symposium|January 1, 1977
Intramolecular interactions, enzyme activity and modelsW N LipscombThe Journal of Biological Chemistry|November 25, 1981
Kinetics of aspartate transcarbamylase from Escherichia coli for the reverse direction of reactionJ Foote, W N LipscombProceedings of the National Academy of Sciences of the United States of America|February 1, 1976
Molecular orbital studies of enzyme activity: catalytic mechanism of serine proteinasesS Scheiner, W N LipscombProceedings of the National Academy of Sciences of the United States of America|June 1, 1993
Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallographyH Kim, W N LipscombJournal of Molecular Biology|August 12, 1994
The crystallization and preliminary X-ray analysis of allosteric chorismate mutaseY Xue, W N LipscombPageof 22