| Literature DB >> 12491538 |
Lukas K Tamm1, Xing Han, Yinling Li, Alex L Lai.
Abstract
Membrane fusion peptides are highly conserved hydrophobic domains of fusion proteins that insert into membranes during membrane fusion. Recent success with solving the structures of the influenza hemagglutinin fusion peptide and some critical mutants of this peptide in membrane environments at high resolution has led to a new understanding of the mechanism of membrane fusion. This review highlights the structures that have been solved and summarizes recent thermodynamic and spectroscopic studies on the interactions of this interesting class of peptides with lipid bilayers. Copyright 2002 Wiley Periodicals, Inc.Entities:
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Year: 2002 PMID: 12491538 DOI: 10.1002/bip.10261
Source DB: PubMed Journal: Biopolymers ISSN: 0006-3525 Impact factor: 2.505