S A Middleton - JoVE Visualize

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Biochemistry|November 15, 1988

Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylaseS A Middleton, E R Kantrowitz

Proceedings of the National Academy of Sciences of the United States of America|August 1, 1986

Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferaseS A Middleton, E R Kantrowitz

Biochemistry|February 21, 1989

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylaseS A Middleton, J W Stebbins, E R Kantrowitz

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.

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.

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.

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.

The Journal of Biological Chemistry|October 15, 1989

Regulatory behavior of Escherichia coli aspartate transcarbamylase altered by site-specific mutation of Tyr240----Phe in the catalytic chainF C Wedler, Y C Hsuanyu, E R Kantrowitz, et al.

Biochemistry|February 21, 1989

Structure of a single amino acid mutant of aspartate carbamoyltransferase at 2.5-A resolution: implications for the cooperative mechanismJ E Gouaux, W N Lipscomb, S A Middleton, et al.

Biochemistry|January 12, 1988

Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylaseM M Ladjimi, S A Middleton, K S Kelleher, et al.

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Showing results (1-10 of 23) with videos related to

Sort By:

Pageof 3

Biochemistry|November 15, 1988

Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylaseS A Middleton, E R Kantrowitz

Proceedings of the National Academy of Sciences of the United States of America|August 1, 1986

Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferaseS A Middleton, E R Kantrowitz

Biochemistry|February 21, 1989

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylaseS A Middleton, J W Stebbins, E R Kantrowitz

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.

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.

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.

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.

The Journal of Biological Chemistry|October 15, 1989

Regulatory behavior of Escherichia coli aspartate transcarbamylase altered by site-specific mutation of Tyr240----Phe in the catalytic chainF C Wedler, Y C Hsuanyu, E R Kantrowitz, et al.

Biochemistry|February 21, 1989

Structure of a single amino acid mutant of aspartate carbamoyltransferase at 2.5-A resolution: implications for the cooperative mechanismJ E Gouaux, W N Lipscomb, S A Middleton, et al.

Biochemistry|January 12, 1988

Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylaseM M Ladjimi, S A Middleton, K S Kelleher, et al.

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