Conformation of gramicidin A channel in phospholipid vesicles: a 13C and 19F nuclear magnetic resonance study.
Identifieur interne : 004995 ( Main/Exploration ); précédent : 004994; suivant : 004996Conformation of gramicidin A channel in phospholipid vesicles: a 13C and 19F nuclear magnetic resonance study.
Auteurs : S. Weinstein ; B A Wallace ; E R Blout ; J S Morrow ; W. VeatchSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1979.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , drug effects : Ion Channels.
- chemical , pharmacology : Manganese, Thulium.
- chemical : Carbon Isotopes, Fluorine, Gramicidin, Lipid Bilayers, Membrane Lipids, Phosphatidylcholines, Spin Labels.
- Magnetic Resonance Spectroscopy, Protein Conformation.
Abstract
We have determined the conformation of the channel-forming polypeptide antibiotic gramicidin A in phosphatidylcholine vesicles by using 13C and 19F NMR spectroscopy. The models previously proposed for the conformation of the dimer channel differ in the surface localization of the NH2 and COOH termini. We have incorporated specific 13C and 19F nuclei at both the NH2, and COOH termini of gramicidin and have used 13C and 19F chemical shifts and spin lattice relaxation time measurements to determine the accessibility of these labels to three paramagnetic NMR probes--two in aqueous solution and one attached to the phosphatidylcholine fatty acid chain9 all of our results indicate that the COOH terminus of gramicidin in the channel is located near the surface of the membrane and the NH2 terminus is buried deep within the lipid bilayer. These findings strongly favor an NH2-terminal to NH2-terminal helical dimer as the major conformation for the gramicidin channel in phosphatidylcholine vesicles.
Url:
PubMed: 92025
PubMed Central: 411546
Affiliations:
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Le document en format XML
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<term>Fluorine</term>
<term>Gramicidin</term>
<term>Ion Channels (drug effects)</term>
<term>Lipid Bilayers</term>
<term>Magnetic Resonance Spectroscopy</term>
<term>Manganese (pharmacology)</term>
<term>Membrane Lipids</term>
<term>Phosphatidylcholines</term>
<term>Protein Conformation</term>
<term>Spin Labels</term>
<term>Thulium (pharmacology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Canaux ioniques ()</term>
<term>Conformation des protéines</term>
<term>Double couche lipidique</term>
<term>Fluor</term>
<term>Gramicidine</term>
<term>Isotopes du carbone</term>
<term>Lipides membranaires</term>
<term>Manganèse (pharmacologie)</term>
<term>Marqueurs de spin</term>
<term>Phosphatidylcholines</term>
<term>Spectroscopie par résonance magnétique</term>
<term>Thulium (pharmacologie)</term>
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<term>Thulium</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Carbon Isotopes</term>
<term>Fluorine</term>
<term>Gramicidin</term>
<term>Lipid Bilayers</term>
<term>Membrane Lipids</term>
<term>Phosphatidylcholines</term>
<term>Spin Labels</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Manganèse</term>
<term>Thulium</term>
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<term>Protein Conformation</term>
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<term>Conformation des protéines</term>
<term>Double couche lipidique</term>
<term>Fluor</term>
<term>Gramicidine</term>
<term>Isotopes du carbone</term>
<term>Lipides membranaires</term>
<term>Marqueurs de spin</term>
<term>Phosphatidylcholines</term>
<term>Spectroscopie par résonance magnétique</term>
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<front><div type="abstract" xml:lang="en"><p>We have determined the conformation of the channel-forming polypeptide antibiotic gramicidin A in phosphatidylcholine vesicles by using 13C and 19F NMR spectroscopy. The models previously proposed for the conformation of the dimer channel differ in the surface localization of the NH2 and COOH termini. We have incorporated specific 13C and 19F nuclei at both the NH2, and COOH termini of gramicidin and have used 13C and 19F chemical shifts and spin lattice relaxation time measurements to determine the accessibility of these labels to three paramagnetic NMR probes--two in aqueous solution and one attached to the phosphatidylcholine fatty acid chain9 all of our results indicate that the COOH terminus of gramicidin in the channel is located near the surface of the membrane and the NH2 terminus is buried deep within the lipid bilayer. These findings strongly favor an NH2-terminal to NH2-terminal helical dimer as the major conformation for the gramicidin channel in phosphatidylcholine vesicles.</p>
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</front>
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<tree><noCountry><name sortKey="Blout, E R" sort="Blout, E R" uniqKey="Blout E" first="E R" last="Blout">E R Blout</name>
<name sortKey="Morrow, J S" sort="Morrow, J S" uniqKey="Morrow J" first="J S" last="Morrow">J S Morrow</name>
<name sortKey="Veatch, W" sort="Veatch, W" uniqKey="Veatch W" first="W" last="Veatch">W. Veatch</name>
<name sortKey="Wallace, B A" sort="Wallace, B A" uniqKey="Wallace B" first="B A" last="Wallace">B A Wallace</name>
<name sortKey="Weinstein, S" sort="Weinstein, S" uniqKey="Weinstein S" first="S" last="Weinstein">S. Weinstein</name>
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