Ligand-linked Structural Changes in the Escherichia coli Biotin Repressor: The Significance of Surface Loops for Binding and Allostery
- 1 September 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 292 (3) , 619-632
- https://doi.org/10.1006/jmbi.1999.3086
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Mapping cyclic nucleotide-induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteasesProtein Science, 2008
- Mapping Conformational Changes in a Protein: Application of a Protein Footprinting Technique to cAMP-Induced Conformational Changes in cAMP Receptor ProteinBiochemistry, 1997
- Crystal Structure of a Group I Ribozyme Domain: Principles of RNA PackingScience, 1996
- [3] Structure and energy change in hemoglobin by hydrogen exchange labelingPublished by Elsevier ,1994
- Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequenceBiochemistry, 1993
- [19] Hydroxyl radical footprintingPublished by Elsevier ,1991
- In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenedifluoride membranes: Cleavage at tryptophan residues with 2-(2′-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine to obtain internal amino acid sequenceAnalytical Biochemistry, 1990
- The E. coli bio operon: Transcriptional repression by an essential protein modification enzymeCell, 1989
- DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of EscherichiaGene, 1986
- The birA gene of Escherichia coli encodes a biotin holoenzyme synthetaseJournal of Molecular Biology, 1981