Showing results (91-100 of 131) with videos related to

Sort By:
Pageof 14
Nature Structural Biology|April 27, 2001
Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylaseC P Macol, H Tsuruta, B Stec, et al.
Journal of Molecular Biology|July 5, 1990
Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylaseP Tauc, P Vachette, S A Middleton, et al.
The Journal of Biological Chemistry|October 15, 1989
Site-specific mutation of Tyr240----Phe in the catalytic chain of Escherichia coli aspartate transcarbamylase. Consequences for kinetic mechanismY Hsuanyu, F C Wedler, E R Kantrowitz, et al.
Chemosphere|April 16, 2013
Solubilization of phenanthrene above cloud point of Brij 30: a new application in biodegradationT Pantsyrnaya, S Delaunay, J L Goergen, et al.
The Journal of Biological Chemistry|January 8, 2000
Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylaseJ B Sakash, R S Chan, H Tsuruta, et al.
Biochemistry|November 1, 1988
Function of arginine-166 in the active site of Escherichia coli alkaline phosphataseA Chaidaroglou, D J Brezinski, S A Middleton, et al.
Protein Science : a Publication of the Protein Society|July 1, 1999
The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativityC Macol, M Dutta, B Stec, et al.
The Journal of Biological Chemistry|May 16, 2001
Domain bridging interactions. A necessary contribution to the function and structure of Escherichia coli aspartate transcarbamoylaseJ B Sakash, M K Williams, H Tsuruta, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 1, 1980
Isolation and preliminary characterization of single amino acid substitution mutants of aspartate carbamoyltransferaseE R Kantrowitz, J Foote, H W Reed, et al.
Biochimica Et Biophysica Acta|March 16, 1989
Kinetic consequences of site-specific mutation of Glu-239----Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzymeY Hsuanyu, F C Wedler, S A Middleton, et al.
Pageof 14