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On the Structure of the Helical N‐Terminus in Alamethicin—α‐Helix or 3 10 ‐Helix?
Author(s) -
Butters Thomas,
Hütter Peter,
Jung Günther,
Pauls Norbert,
Schmitt Heribert,
Sheldrick George M.,
Winter Werner
Publication year - 1981
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.198108891
Subject(s) - alamethicin , helix (gastropod) , triple helix , chemistry , alpha helix , crystallography , stereochemistry , circular dichroism , biology , biochemistry , membrane , ecology , lipid bilayer , snail
The crystal structure of the helical undecapeptide (1) , a model of the N ‐terminal alamethicin helix , suggests that no 3 10 ‐ but an α‐helix conformation is most probably present in the antibiotics alamethicin, trichotoxin, and suzukacillin. The nine N ‐terminal amino acids of (1) are part of an α‐helix.