title: Experimental and computational studies of determinants of membrane-protein folding.
abstract: Recent experiments and analysis have demonstrated the important roles of hydrogen bonding and polar-polar interactions in driving transmembrane helix-helix association. Further details of the energetics of helix-helix association and interhelical packing geometry are being mapped out. Many sequence motifs and a few spatial motifs promoting helical associations have also been identified.
authors.affiliation: Department of Bioengineering, University of Illinois at Chicago, SEO 218, MC-063 851, South Morgan Street, Chicago, IL 60607, USA. jiliang@uic.edu
authors.forename: Jie
authors.initials: J
authors.lastname: Liang
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D006860:Hydrogen Bonding; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D008565:Membrane Proteins