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- W2114485364 abstract "ABSTRACT Melittin, the main hemolytic component of honeybee venom, is unfolded in an aqueous environment and folds into an α‐helical conformation in a lipid environment. Membrane fluidity is known to affect the activity and structure of melittin. By combining two structurally sensitive optical methods, circular dichroism (CD) and deep‐ultraviolet resonance Raman spectroscopy (dUVRR), we have identified distinct structural fluctuations in melittin correlated with increased and decreased 1,2‐dimyristoyl‐sn‐glycero‐3‐phosphocholine bilayer fluidities. CD spectra have reduced intensity at temperatures above 22°C and high concentrations of the cholesterol analog 5α‐cholestan‐3β‐ol indicating distortions in the α‐helical structure under these conditions. No increase in the amide S is observed in the temperature‐dependent dUVRR spectra, suggesting an increase in 3 10 ‐helical structure with increasing temperatures above 22°C. However, incorporation of 25 mol% 5α‐cholestan‐3β‐ol resulted in a small increase in the amide S intensity indicating partial unfolding of melittin. © 2014 Wiley Periodicals, Inc. Biopolymers 101: 895–902, 2014." @default.
- W2114485364 created "2016-06-24" @default.
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- W2114485364 creator A5059421671 @default.
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- W2114485364 date "2014-05-27" @default.
- W2114485364 modified "2023-10-16" @default.
- W2114485364 title "Effects of fluidity on the ensemble structure of a membrane embedded α‐helical peptide" @default.
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- W2114485364 doi "https://doi.org/10.1002/bip.22472" @default.
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