Cation-π Interactions as Determinants for Binding of the Compatible Solutes Glycine Betaine and Proline Betaine by the Periplasmic Ligand-binding Protein ProX from Escherichia coli
Open Access
- 1 February 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (7) , 5588-5596
- https://doi.org/10.1074/jbc.m309771200
Abstract
No abstract availableKeywords
This publication has 73 references indexed in Scilit:
- Ecological significance of compatible solute accumulation by micro-organisms: from single cells to global climateFEMS Microbiology Reviews, 2000
- The Protein Data BankNucleic Acids Research, 2000
- Osmoadaptation and osmoregulation in archaeaFrontiers in Bioscience-Landmark, 2000
- Multiple open forms of ribose-binding protein trace the path of its conformational changeJournal of Molecular Biology, 1998
- REGULATION OF GENE EXPRESSION BY HYPERTONICITYAnnual Review of Physiology, 1997
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- On the use of the mergingRfactor as a quality indicator for X-ray dataJournal of Applied Crystallography, 1997
- Isolation and Sequencing of Escherichia coli Gene proP Reveals Unusual Structural Features of the Osmoregulatory Proline/Betaine transporter, ProPJournal of Molecular Biology, 1993
- Basic local alignment search toolJournal of Molecular Biology, 1990
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983