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• W2020219857 startingPage "117" @default.
• W2020219857 abstract "Gramicidin A (gA) is a linear pentadecapeptide, which exhibits various conformations depending on the environment. The conformational behavior of gA in spherical and rod-shaped cationic micelles formed by cetyltrimethylammonium bromide (CTAB) surfactant has been studied using circular dichroism (CD) and fluorescence spectroscopy, and a probable structure of gramicidin A in CTAB media has been proposed. A CD study shows that gramicidin A assumes beta(6.3) helical structure in cationic spherical as well as rod-shaped CTAB micellar media. Modeling studies show the flexibility of the side chain conformation particularly in tryptophan-9. Study of intrinsic fluorescence of tryptophans in gramicidin A indicates three distinct environments for the four-tryptophan residues in CTAB media." @default.
• W2020219857 created "2016-06-24" @default.
• W2020219857 creator A5025076124 @default.
• W2020219857 creator A5085513768 @default.
• W2020219857 creator A5085789773 @default.
• W2020219857 date "2003-05-01" @default.
• W2020219857 modified "2023-09-27" @default.
• W2020219857 title "Conformation of gramicidin-A in CTAB micellar media" @default.
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• W2020219857 doi "https://doi.org/10.1016/s1011-1344(03)00055-1" @default.
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• W2020219857 hasPublicationYear "2003" @default.
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