Dynamic transition of α-helix to β-sheet structure in linear surfactin correlating to critical micelle concentration View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-09

AUTHORS

Mohamad Osman, Yutaka Ishigami, Keiichiro Ishikawa, Yasuko Ishizuka, Holm Holmsen

ABSTRACT

Linear heptapeptide surfactin was prepared by alkaline cleavage of the lactone ring of cyclic surfactin. The structure of linear surfactin was characterised and confirmed by FAB-mass-spectroscopy, FT-IR and HPLC analysis. It was found that linear surfactin easily forms micelles in aqueous solutions by coordinating β-sheet formation from α-helical monomolecules, and the cmc value found to be 1.28×10−5 M. The CD spectra indicates conformational change of linear surfactin from α-helical below cmc to β-sheet above cmc. More... »

PAGES

913-918

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00128624

DOI

http://dx.doi.org/10.1007/bf00128624

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1047056533


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