Intrinsic rectification of ion flux in alamethicin channels: studies with an alamethicin dimer
| Autor: | Karin A. Crowhurst, D. C. J. Jaikaran, P. C. Biggin, Mark S.P. Sansom, G. A. Woolley, Linda Lien, J. Breed, A. Schultz |
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| Jazyk: | angličtina |
| Předmět: |
Potassium Channels
Lipid Bilayers Molecular Sequence Data Static Electricity Biophysics Analytical chemistry Gating Models Biological Protein Structure Secondary Ion Membrane Potentials Potassium Chloride chemistry.chemical_compound Rectification Static electricity Amino Acid Sequence Alamethicin Lipid bilayer Membrane potential Chemistry Potassium channel Models Structural Kinetics Chemical physics Phosphatidylcholines Thermodynamics Dimerization Ion Channel Gating Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0006-3495 |
| DOI: | 10.1016/S0006-3495(97)78109-8 |
| Popis: | Covalent dimers of alamethicin form conducting structures with gating properties that permit measurement of current-voltage (I-V) relationships during the lifetime of a single channel. These I-V curves demonstrate that the alamethicin channel is a rectifier that passes current preferentially, with voltages of the same sign as that of the voltage that induced opening of the channel. The degree of rectification depends on the salt concentration; single-channel I-V relationships become almost linear in 3 M potassium chloride. These properties may be qualitatively understood by using Poisson-Nernst-Planck theory and a modeled structure of the alamethicin pore. |
| Databáze: | OpenAIRE |
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