title: Dynamic helix interactions in transmembrane signaling.
abstract: Studying how protein transmembrane domains transmit signals across membranes is beset by unique challenges. Here, we discuss the circumstances that have led to success and reflect on what has been learned from these examples. Such efforts suggest that some of the most interesting properties of transmembrane helix interactions may be the least amenable to study by current techniques.
authors.affiliation: Department of Chemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
authors.forename: Erin E
authors.initials: EE
authors.lastname: Matthews
authors.forename: Manuela
authors.initials: M
authors.lastname: Zoonens
authors.forename: Donald M
authors.initials: DM
authors.lastname: Engelman
mesh_terms: D002462:Cell Membrane / Q000737:chemistry / Q000235:genetics; D008051:Lipid Bilayers / Q000737:chemistry; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008823:Micelles; D008958:Models, Molecular; D008961:Models, Structural; D009154:Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins; D008823:Micelles; D011956:Receptors, Cell Surface; D011505:Protein-Tyrosine Kinases