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

✍ Scribed by Mohamad Osman; Yutaka Ishigami; Keiichiro Ishikawa; Yasuko Ishizuka; Holm Holmsen

Book ID: 104633185
Publisher: Springer Netherlands
Year: 1994
Tongue: English
Weight: 421 KB
Volume: 16
Category: Article
ISSN: 0141-5492
DOI: 10.1007/bf00128624

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✦ Synopsis

Linear heptapeptide surfactin was prepared by alkaline cleavage of the lactone ring of cyclic surfactin. The structure of linear surfactin was eharaeterised and confLrmed by FAB-mass-spectroscopy, FT-IR and HPLC analysis. It was found that linear suffactin easily forms micelles in aqueous solutions by coordinating ~shect formstion from a-helical monomoleeules, and the cme value found to be 1.28x10 5 M. The CD spectra indicates conformational change of linear surfactin from a-helical below emc to ~sheet above cane.

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Kinetics of coil to α-helix to β-structu

Kinetics of coil to α-helix to β-structure transitions of poly(L-ornithine) in low concentrations of sodium dodecyl sulfate

✍ Kunio Takeda 📂 Article 📅 1985 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 620 KB

Conformational changes of poly(i-ornithine) [(Orn),] were studied in a sodium dodecyl sulfate (NaDodSO,) solution by CD. (Orn), adopted a n unstable and a stable helical structure below and above the NaDodSO, concentration range where &structure was favored, respectively. CD stopped-flow was used to