Mechanism of Na+ binding to thrombin resolved by ultra-rapid kinetics
- 1 October 2007
- journal article
- other
- Published by Elsevier in Biophysical Chemistry
- Vol. 131 (1-3) , 111-114
- https://doi.org/10.1016/j.bpc.2007.09.009
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Demonstration of Long-Range Interactions in a PDZ Domain by NMR, Kinetics, and Protein EngineeringStructure, 2006
- Role of Na+and K+in Enzyme FunctionPhysiological Reviews, 2006
- A Structural Perspective on Enzymes Activated by Monovalent CationsJournal of Biological Chemistry, 2006
- The Cavity and Pore Helices in the KcsA K + Channel: Electrostatic Stabilization of Monovalent CationsScience, 1999
- Mechanisms of Monovalent Cation Action in Enzyme Catalysis: The Tryptophan Synthase α-, β-, and αβ-ReactionsBiochemistry, 1999
- Mechanisms of Monovalent Cation Action in Enzyme Catalysis: The First Stage of the Tryptophan Synthase β-ReactionBiochemistry, 1999
- Kinetic Mechanism of Tritrichomonas foetus Inosine 5‘-Monophosphate DehydrogenaseBiochemistry, 1999
- Evidence for barrier-limited protein folding kinetics on the microsecond time scaleNature Structural & Molecular Biology, 1998
- Metal-Ion-Mediated Allosteric Triggering of Yeast Pyruvate Kinase. 1. A Multidimensional Kinetic Linked-Function AnalysisBiochemistry, 1997
- An allosteric switch controls the procoagulant and anticoagulant activities of thrombin.Proceedings of the National Academy of Sciences, 1995