Thermodynamics of the Interaction of the Escherichia coli Regulatory Protein TyrR with DNA Studied by Fluorescence Spectroscopy-Reference-Cited by-同舟云学术

Thermodynamics of the Interaction of the Escherichia coli Regulatory Protein TyrR with DNA Studied by Fluorescence Spectroscopy

Published:1998-04-30 Issue:20 Volume:37 Page:7431-7443
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bailey Michael F.¹,Davidson Barrie E.¹,Haralambidis Jim¹,Kwok Terry¹,Sawyer William H.¹

Affiliation:

1. The Russell Grimwade School of Biochemistry and Molecular Biology, and The Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville, Victoria 3052, Australia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi972854a

Reference43 articles.

1. Purification of the Escherichia coli regulatory protein TyrR and analysis of its interactions with ATP, tyrosine, phenylalanine, and tryptophan.

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1. Thermodynamic Dissection of the Polymerizing and Editing Modes of a DNA Polymerase;Journal of Molecular Biology;2004-02

2. Solution structure of the DNA-binding domain of the TyrR protein ofHaemophilus influenzae;Protein Science;2001-03

3. Major Groove Recognition by Three-stranded β-Sheets: Affinity Determinants and Conserved Structural Features;Journal of Molecular Biology;2000-07

4. Distances between DNA and ATP Binding Sites in the TyrR−DNA Complex;Biochemistry;2000-04-21

5. The influence of ATP on the binding of aromatic amino acids to the ligand response domain of the tyrosine repressor ofHaemophilus influenzae;FEBS Letters;2000-02-02