title: Shorter side chains optimize helix-helix packing.
abstract: A systematic study of helix-helix packing in a comprehensive database of protein structures revealed that the side chains inside helix-helix interfaces on average are shorter than those in the noninterface parts of the helices. The study follows our earlier study of this effect in transmembrane helices. The results obtained on the entire database of protein structures are consistent with those obtained on the transmembrane helices. The difference in the length of interface and noninterface side chains is small but statistically significant. It indicates that helices, if viewed along their main axis, statistically are not circular, but have a flattened interface. This effect brings the helices closer to each other and creates a tighter structural packing. The results provide an interesting insight into the aspects of protein structure and folding.
authors.affiliation: Department of Biochemistry, Weill Medical College of Cornell University, New York, New York 10021, USA.
authors.forename: Sulin
authors.initials: S
authors.lastname: Jiang
authors.forename: Ilya A
authors.initials: IA
authors.lastname: Vakser
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D008962:Models, Theoretical; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry
chemical_list: D000596:Amino Acids; D011506:Proteins