Sequence and conformational preferences at termini of α‐helices in membrane proteins: Role of the helix environment
Shelar A, Bansal M. Sequence and conformational preferences at termini of α‐helices in membrane proteins: Role of the helix environment. Proteins Structure Function And Bioinformatics 2014, 82: 3420-3436. PMID: 25257385, DOI: 10.1002/prot.24696.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsComputational BiologyConserved SequenceDatabases, ProteinHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane ProteinsModels, BiologicalProtein ConformationProtein FoldingProtein StabilityProtein Structure, SecondarySoftware ValidationTerminology as TopicConceptsMembrane proteinsSequence preferenceΑ-helixC-terminusHelical membrane proteinsCommon secondary structural elementsHelix terminiStructural motifsSecondary structural elementsSecondary structure predictionRat neurotensin receptorTransmembrane helicesMembrane environmentHelix bundleSequencing studiesHelical positionsAmino acidsProteinStructure predictionTerminusMembrane coreGlobular proteinsMotifHelixConformational preferences
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