title: Forster resonance energy transfer measurements of transmembrane helix dimerization energetics.
abstract: Lateral interactions between hydrophobic transmembrane (TM) helices in membranes underlie the folding of multispan membrane proteins and signal transduction by receptor tyrosine kinases (RTKs). Quantitative measurements of dimerization energetics in membranes are required to uncover the physical principles behind these processes. Here, we overview how FRET measurements can be used to determine the thermodynamics of TM helix homo- and heterodimerization in vesicles and in supported bilayers. Such measurements can shed light on the molecular mechanism behind pathologies arising due to single-amino acid mutations in membrane proteins.
authors.affiliation: Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland 21218, USA.
authors.forename: Mikhail
authors.initials: M
authors.lastname: Merzlyakov
authors.forename: Kalina
authors.initials: K
authors.lastname: Hristova
mesh_terms: D019281:Dimerization; D031541:Fluorescence Resonance Energy Transfer; D008051:Lipid Bilayers; D011506:Proteins / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D008051:Lipid Bilayers; D011506:Proteins