title: Membrane proteins: shaping up.
abstract: Over recent years, much progress has been made in the identification and characterization of factors involved in the biosynthesis of integral membrane proteins of the helix-bundle type. In addition, our knowledge of membrane protein structure and the forces stabilizing helix-helix interactions in a lipid environment is expanding rapidly. However, it is still not clear how a membrane protein folds into its final form in vivo, nor what constraints there are on the folded structure that results from the mechanistic details of translocon-mediated assembly rather than simply from the thermodynamics of protein-lipid interactions.
authors.affiliation: Department Molecular Biophysics and Biochemistry, Yale University, Bass 429, 266 Whitney Avenue, New Haven, CT 06520, USA.
authors.forename: Chen-Ni
authors.initials: CN
authors.lastname: Chin
authors.forename: Gunnar
authors.initials: G
authors.lastname: von Heijne
authors.forename: Jan-Willem L
authors.initials: JW
authors.lastname: de Gier
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021381:Protein Transport / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins