Ion channel stabilization of synthetic alamethicin analogs by rings of inter-helix H-bonds
- 1 April 1996
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 70 (4) , 1669-1675
- https://doi.org/10.1016/s0006-3495(96)79729-1
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Conformational study of a synthetic analogue of alamethicin Influence of the conformation on ion-channel lifetimesInternational Journal of Peptide and Protein Research, 2009
- Collisions between helical peptides in membranes monitored using electron paramagnetic resonance: evidence that alamethicin is monomeric in the absence of a membrane potentialBiophysical Journal, 1994
- Alamethicin: A Peptide Model for Voltage Gating and Protein-Membrane InteractionsAnnual Review of Biophysics, 1994
- Effects of polycations on ion channels formed by neutral and negatively charged alamethicinsEuropean Biophysics Journal, 1994
- Structure and function of channel-forming peptaibolsQuarterly Reviews of Biophysics, 1993
- Prolines are not essential residues in the "barrel-stave" model for ion channels induced by alamethicin analoguesBiophysical Journal, 1992
- Membrane-modifying properties of the pore-forming peptaibols saturnisporin SA IV and harzianin HA VFEMS Microbiology Letters, 1992
- Model ion channels: Gramicidin and alamethicinThe Journal of Membrane Biology, 1992
- The biophysics of peptide models of ion channelsProgress in Biophysics and Molecular Biology, 1991
- Circular dichroic analysis of protein conformation: Inclusion of the β-turnsAnalytical Biochemistry, 1978