Helical Behavior of the Interdomain Linker of the Escherichia coli AraC Protein
Author:
Affiliation:
1. Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, United States
Funder
Department of Biology, Johns Hopkins University
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00234
Reference36 articles.
1. The Linker between the Dimerization and Catalytic Domains of the CheA Histidine Kinase Propagates Changes in Structure and Dynamics That Are Important for Enzymatic Activity
2. Dynamic Allostery: Linkers Are Not Merely Flexible
3. Determination of the Individual Roles of the Linker Residues in the Interdomain Motions of Calmodulin Using NMR Chemical Shifts
4. Control of protein functional dynamics by peptide linkers
5. Further evidence for positive control of the l-arabinose system by gene araC
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1. Atomic force microscopy measurements and model of DNA bending caused by binding of AraC protein;Journal of Molecular Recognition;2022-09-30
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3. Allosteric regulation within the highly interconnected structural scaffold of AraC / XylS homologs tolerates a wide range of amino acid changes;Proteins: Structure, Function, and Bioinformatics;2021-08-16
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