Studies of the dimerization of transmembrane (TM) helices have been ongoing for many
years now, and have provided clues to the fundamental principles behind membrane protein …

Interaction between transmembrane helices often determines biological activity of
membrane proteins. Bitopic proteins, a broad subclass of membrane proteins, form dimers …

Production of integral membrane proteins (IMPs) in a folded state is a key prerequisite for
their functional and structural studies. In cell-free (CF) expression systems membrane …

Folding of polytopic transmembrane proteins involves interactions of individual
transmembrane helices, and multiple TM helix–helix interactions need to be controlled and …

The extraction of membrane proteins from their native environment by detergents is central
to their biophysical characterization. Recent studies have emphasized that detergents may …

Some pathogenic mutations associated with Alzheimer's disease are thought to affect
structural-dynamic properties and the lateral dimerization of amyloid precursor protein (APP) …

Receptor tyrosine kinases of the human epidermal growth factor receptor (HER or ErbB)
family transduce biochemical signals across plasma membrane, playing a significant role in …

Specific helix–helix interactions between the single-span transmembrane domains of
receptor tyrosine kinases are believed to be important for their lateral dimerization and …

Single‐pass transmembrane receptors are involved in essential processes of both
physiological and pathological nature and represent more than 1300 proteins in the human …

Background: Dimerization regulates activation of PDGF receptor in signal transduction.
Results: The transmembrane segment of PDGFR forms a left-handed helical dimer, which …