Data on diverse roles of helix perturbations in membrane proteins
Shelar A, Bansal M. Data on diverse roles of helix perturbations in membrane proteins. Data In Brief 2016, 9: 781-802. PMID: 27844046, PMCID: PMC5099277, DOI: 10.1016/j.dib.2016.10.023.Peer-Reviewed Original ResearchInter-helical interactionsMembrane proteinsHelix perturbationTM helicesMembrane protein familyProtein familyHydrophobic residuesDiverse rolesKinked geometryΠ-helixOligomer formationBackbone torsion anglesProteinHelixStructural variationsHelical conformationDistinct typesBilayersResiduesStrong evidenceLinear αRoleHelix perturbations in membrane proteins assist in inter-helical interactions and optimal helix positioning in the bilayer
Shelar A, Bansal M. Helix perturbations in membrane proteins assist in inter-helical interactions and optimal helix positioning in the bilayer. Biochimica Et Biophysica Acta 2016, 1858: 2804-2817. PMID: 27521749, DOI: 10.1016/j.bbamem.2016.08.003.Peer-Reviewed Original ResearchConceptsInter-helical interactionsMembrane proteinsTM regionHelix perturbationTM helicesΠ-helixDistinct sequence signaturesIntegral membrane proteinsLow sequence identityHeme-copper oxidasesTransmembrane helicesProtein functionSequence signaturesSequence identityHydrophobic mismatchΑ-helixProtein chainsAmino acidsHelical fragmentsCopper oxidasesProteinHelix terminiHelixTerminusBilayers