1998
Structure-based prediction of the stability of transmembrane helix–helix interactions: The sequence dependence of glycophorin A dimerization
MacKenzie K, Engelman D. Structure-based prediction of the stability of transmembrane helix–helix interactions: The sequence dependence of glycophorin A dimerization. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 3583-3590. PMID: 9520409, PMCID: PMC19879, DOI: 10.1073/pnas.95.7.3583.Peer-Reviewed Original ResearchConceptsHelix-helix interactionsTransmembrane helix-helix associationTransmembrane helix-helix interactionsHelix-helix associationSingle-point mutantsStructure-based predictionTransmembrane domainMembrane proteinsDimer interfaceDimerization propensitySide-chain hydrophobicityDimer stabilityPoint mutationsSteric clashesMultiple mutationsMutationsSequence dependenceCompensatory effectFavorable van der Waals interactionsMutantsFoldingProteinInteractionDimerizationGlycophorin
1996
Surface point mutations that significantly alter the structure and stability of a protein's denatured state
Smith C, Bu Z, Engelman D, Regan L, Anderson K, Sturtevant J. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Science 1996, 5: 2009-2019. PMID: 8897601, PMCID: PMC2143264, DOI: 10.1002/pro.5560051007.Peer-Reviewed Original ResearchConceptsPoint mutationsDenatured stateStopped-flow fluorescenceDenaturant concentrationSolvent-exposed sitesStreptococcal protein GMutantsG mutantTertiary structureGuHCl denaturationEquilibrium intermediatesPosition 53B1 domainProteinCircular dichroismMutationsProtein GGuanidine hydrochlorideSmall-angle X-ray scatteringStructural implicationsX-ray scatteringFluorescenceThrRadius of gyrationDenaturants