title: Sequence motifs, polar interactions and conformational changes in helical membrane proteins.
abstract: The alpha helices of transmembrane proteins interact to form higher order structures. These interactions are frequently mediated by packing motifs (such as GxxxG) and polar residues. Recent structural data have revealed that small sidechains are able to both stabilize helical membrane proteins and allow conformational changes in the structure. The strong interactions involving polar sidechains often contribute to protein misfolding or malfunction.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, PO Box 208114, New Haven, CT 06520-8114, USA.
authors.forename: A Rachael
authors.initials: AR
authors.lastname: Curran
authors.forename: Donald M
authors.initials: DM
authors.lastname: Engelman
mesh_terms: D020816:Amino Acid Motifs; D006860:Hydrogen Bonding; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D008565:Membrane Proteins