Cation Control in Functional Helical Programming: Structures of a D,L-Peptide Ion Channel

Cation Control in Functional Helical Programming: Structures of a D,L-Peptide Ion Channel

Variable ion channels: A 22mer peptide derived from the D,L‐peptide gramicidin A changes from an inactive to a highly ion‐channel‐active conformation (see picture). The helical structure of the active and inactive conformations was characterized by NMR spectroscopy and circular dichroism; conductanc...

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Veröffentlicht in:Angewandte Chemie International Edition 2002-11, Vol.41 (21), p.4062-4065
Hauptverfasser: Arndt, Hans-Dieter, Bockelmann, Dirk, Knoll, Andrea, Lamberth, Stefanie, Griesinger, Christian, Koert, Ulrich
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Binding Sites
Cations, Monovalent - metabolism
Cations, Monovalent - pharmacology
Cesium - metabolism
Cesium - pharmacology
Circular Dichroism
conformational analysis
Gramicidin - chemistry
Gramicidin - metabolism
Ion Channel Gating - drug effects
ion channels
Ion Channels - chemistry
Ion Channels - metabolism
Ion Transport - drug effects
Kinetics
Magnetic Resonance Spectroscopy
Models, Molecular
NMR spectroscopy
peptides
Protein Conformation - drug effects
Structure-Activity Relationship
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Zusammenfassung:Variable ion channels: A 22mer peptide derived from the D,L‐peptide gramicidin A changes from an inactive to a highly ion‐channel‐active conformation (see picture). The helical structure of the active and inactive conformations was characterized by NMR spectroscopy and circular dichroism; conductance measurements led to the conclusion that there are two symmetrical binding sites for the Cs atom in the active form.
ISSN:1433-7851
1521-3773
DOI:10.1002/1521-3773(20021104)41:21<4062::AID-ANIE4062>3.0.CO;2-U