Acetylcholinesterase: Effects of Ionic Strength and Dimerization on the Rate Constants
- 1 January 1994
- journal article
- research article
- Published by Wiley in Israel Journal of Chemistry
- Vol. 34 (2) , 151-158
- https://doi.org/10.1002/ijch.199400020
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Multiple‐site titration and molecular modeling: Two rapid methods for computing energies and forces for ionizable groups in proteinsProteins-Structure Function and Bioinformatics, 1993
- Acetylcholinesterase: electrostatic steering increases the rate of ligand bindingBiochemistry, 1993
- Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding ProteinScience, 1991
- The nature of protein dipole moments: experimental and calculated permanent dipole of .alpha.-chymotrypsinBiochemistry, 1989
- Diffusional dynamics of ligand-receptor associationThe Journal of Physical Chemistry, 1986
- Calculation of the electric potential in the active site cleft due to α-helix dipolesJournal of Molecular Biology, 1982
- Kinetics of acetylthiocholine binding to electric eel acetylcholinesterase in glycerol/water solvents of increased viscosity Evidence for a diffusion-controlled reactionBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligandsBiochemistry, 1980
- Brownian dynamics with hydrodynamic interactionsThe Journal of Chemical Physics, 1978
- Neuromuscular Transmission—Enzymatic Destruction of AcetylcholinePublished by Springer Nature ,1974