Ontology highlight
ABSTRACT:
SUBMITTER: Quint S
PROVIDER: S-EPMC2955363 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Quint Stefan S Widmaier Simon S Minde David D Minde David D Hornburg Daniel D Langosch Dieter D Scharnagl Christina C
Biophysical journal 20101001 8
The transmembrane domains (TMDs) of membrane-fusogenic proteins contain an overabundance of β-branched residues. In a previous effort to systematically study the relation among valine content, fusogenicity, and helix dynamics, we developed model TMDs that we termed LV-peptides. The content and position of valine in LV-peptides determine their fusogenicity and backbone dynamics, as shown experimentally. Here, we analyze their conformational dynamics and the underlying molecular forces using molec ...[more]