Interaction of fusogenic or membrane-perturbing peptides with lipid bilayers often involves drastic rearrangements of the membrane structure, with redistribution of lipids, inducement of bilayer curvature, or formation of nonbilayer or multibilayer structures. Fluorescence (or Forster) Resonance Energy Transfer (FRET) is a photophysical technique which has an acute sensitivity to distances in the nanometer range, and, as such, is particularly suited to probe alterations in membrane organization in this length scale. This article reviews methods and selected applications of FRET in this field, from the now classic (fusion induced) lipid-mixing assay to examples where kinetic modeling of FRET enables the recovery of topological information.
Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.