Zur Struktur des helicalen N-Terminus im Alamethicin – α-Helix oder 310-Helix?
Author:
Publisher
Wiley
Subject
General Medicine
Reference21 articles.
1. Analysis of the multi-pore system of alamethicin in a lipid membrane
2. Alamethicin-induced single channel conductance fluctuations in biological membranes
3. Structural and membrane modifying properties of suzukacillin, a peptide antibiotic related to alamethicin
4. Trichotoxin A-40, a new membrane-exciting peptide. Part B. Voltage-dependent pore formation in bilayer lipid membranes and comparison with other alamethicin analogues
5. Conformational Changes of Alamethicin Induced by Solvent and Temperature. A 13C-NMR and Circular-Dichroism Study
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3. Heterogeneity of packing: Structural approach;Protein Science;1998-04
4. Design and synthesis of novel nonpolar host peptides for the determination of the 310- and α-helix compatibilities of α-amino acid buildig blocks: An assessment of α,α-disubstituted glycines;Biopolymers;1997-10-15
5. Molecular Dynamics Simulation of Conformational Flexibility of Alamethicin Fragments in Aqueous and Membranous Environment;Journal of Biomolecular Structure and Dynamics;1996-12
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