Is the Gramicidin A Transmembrane Channel Single-Stranded or Double-Stranded Helix? A Simple Unequivocal Determination
Author:
Affiliation:
1. Laboratory of Molecular Biophysics, University of Alabama School of Medicine, Birmingham 35294
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference31 articles.
1. APELL, H.J., FORMATION OF ION CHANNELS BY A NEGATIVELY CHARGED ANALOG OF GRAMICIDIN-A, JOURNAL OF MEMBRANE BIOLOGY 31: 171 (1977).
2. BAMBERG, E, TEMPERATURE-DEPENDENT PROPERTIES OF GRAMICIDIN A CHANNELS, BIOCHIMICA ET BIOPHYSICA ACTA 367: 127 (1974).
3. BAMBERG, E, CHANNEL FORMATION KINETICS OF GRAMICIDIN-A IN LIPID BILAYER MEMBRANES, JOURNAL OF MEMBRANE BIOLOGY 11: 177 (1973).
4. BAMBERG, E, BLOCKING OF GRAMICIDIN CHANNEL BY DIVALENT-CATIONS, JOURNAL OF MEMBRANE BIOLOGY 35: 351 (1977).
5. BAMBERG, E, STRUCTURE OF GRAMICIDIN A CHANNEL - DISCRIMINATION BETWEEN PI-L,D AND BETA-HELIX BY ELECTRICAL MEASUREMENTS WITH LIPID BILAYER MEMBRANES, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 74: 2402 (1977).
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