Conformational transitions of membrane-bound HIV-1 fusion peptide.

@article{SezCirin2002ConformationalTO,
  title={Conformational transitions of membrane-bound HIV-1 fusion peptide.},
  author={Asier S{\'a}ez-Ciri{\'o}n and Jos{\'e} Luis Nieva},
  journal={Biochimica et biophysica acta},
  year={2002},
  volume={1564 1},
  pages={57-65}
}
The human immunodeficiency virus type-1 (HIV-1) fusion peptide (FP) functions as a non-constitutive membrane anchor that translocates into membranes during envelope glycoprotein-induced fusion. Here, by means of infrared spectroscopy (IR) and of various bilayer-perturbation assays, we describe the peptide conformations that are accessible to its membrane-bound state and the transitions occurring between them. The peptide underwent a conformational transition from a predominantly alpha-helical… CONTINUE READING