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Structural plasticity of the feline leukaemia virus fusion peptide: a circular dichroism study
Author(s) -
Davies Sarah M.A,
Kelly Sharon M,
Price Nicholas C,
Bradshaw Jeremy P
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00274-9
Subject(s) - circular dichroism , random coil , protein secondary structure , peptide , lipid bilayer fusion , biophysics , chemistry , fusion , crystallography , lipid bilayer , membrane , biochemistry , biology , linguistics , philosophy
The secondary structure of the feline leukaemia virus (FeLV) fusion peptide was investigated using circular dichroism (CD). Our results show that this peptide can readily flip between random, α‐helical and β‐sheet conformations, depending upon its environment. The CD spectrum changes from one characteristic of random coil to predominantly β‐sheet type, and finally to that showing the characteristics of α‐helical structure on moving from an aqueous solvent, through several increasingly hydrophobic systems, to a highly hydrophobic solvent. Electron microscopy confirmed the presence of β structure. We propose that the structural plasticity demonstrated here is crucial to the ability of the fusion peptide to perturb lipid bilayers, and thus promote membrane fusion.