title: Data on diverse roles of helix perturbations in membrane proteins.
abstract: The various structural variations observed in TM helices of membrane proteins have been deconstructed into 9 distinct types of helix perturbations. These perturbations are defined by the deviation of TM helices from the predominantly observed linear α-helical conformation, to form 310- and π-helices, as well as adopting curved and kinked geometries. The data presented here supplements the article 'Helix perturbations in Membrane Proteins Assist in Inter-helical Interactions and Optimal Helix Positioning in the Bilayer' (A. Shelar, M. Bansal, 2016) [1]. This data provides strong evidence for the role of various helix perturbations in influencing backbone torsion angles of helices, mediating inter-helical interactions, oligomer formation and accommodation of hydrophobic residues within the bilayer. The methodology used for creation of various datasets of membrane protein families (Sodium/Calcium exchanger and Heme Copper Oxidase) has also been mentioned.
authors.affiliation: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, Karnataka, India.
authors.forename: Ashish
authors.initials: A
authors.lastname: Shelar
authors.affiliation: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, Karnataka, India.
authors.forename: Manju
authors.initials: M
authors.lastname: Bansal
keywords: Helix interactions; Helix kink; Membrane proteins