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Stabilizing effects of 2-methylalanine residues on β-turns and α-helices

✍ Scribed by G. Jung; R. Bosch; E. Katz; H. Schmitt; K.-P. Voges; W. Winter


Publisher
Wiley (John Wiley & Sons)
Year
1983
Tongue
English
Weight
255 KB
Volume
22
Category
Article
ISSN
0006-3525

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✦ Synopsis


An N-terminal rigid a-helical segment is found in the polypeptide antibiotics alamethicin, suzukacillin, and trichotoxin. The a-helix dipole is essential for their voltage-dependent pore formation in lipid bilayer membranes, which is explained by a flip-flop gating mechanism based on dipole-dipole interactions of parallel and antiparallel arranged a-helices within oligomeric structures.


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