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Cation Control in Functional Helical Programming: Structures of a D , L ‐Peptide Ion Channel
Author(s) -
Arndt HansDieter,
Bockelmann Dirk,
Knoll Andrea,
Lamberth Stefanie,
Griesinger Christian,
Koert Ulrich
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20021104)41:21<4062::aid-anie4062>3.0.co;2-u
Subject(s) - ion channel , circular dichroism , peptide , chemistry , ion , gramicidin , crystallography , conductance , stereochemistry , membrane , physics , biochemistry , receptor , organic chemistry , condensed matter physics
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.