2018
Comparing side chain packing in soluble proteins, protein‐protein interfaces, and transmembrane proteins
Gaines JC, Acebes S, Virrueta A, Butler M, Regan L, O'Hern CS. Comparing side chain packing in soluble proteins, protein‐protein interfaces, and transmembrane proteins. Proteins Structure Function And Bioinformatics 2018, 86: 581-591. PMID: 29427530, PMCID: PMC5912992, DOI: 10.1002/prot.25479.Peer-Reviewed Original ResearchConceptsProtein-protein interfacesClass of proteinsTransmembrane proteinSoluble proteinSolvent-inaccessible coreMembrane proteinsProtein classesCore residuesProtein-protein interactionsHigh-resolution crystal structuresHydrophobic core mutationsRelative solvent accessibilityAnalysis of mutationsSide-chain packingProtein complexesNon-core regionsSolvent accessibilityProteinSide-chain conformationsCore mutationsMutationsResiduesSide chains
2014
Intrinsic α‐helical and β‐sheet conformational preferences: A computational case study of alanine
Caballero D, Määttä J, Zhou AQ, Sammalkorpi M, O'Hern CS, Regan L. Intrinsic α‐helical and β‐sheet conformational preferences: A computational case study of alanine. Protein Science 2014, 23: 970-980. PMID: 24753338, PMCID: PMC4088981, DOI: 10.1002/pro.2481.Peer-Reviewed Original Research
2012
The Power of Hard-Sphere Models: Explaining Side-Chain Dihedral Angle Distributions of Thr and Val
Zhou AQ, O'Hern CS, Regan L. The Power of Hard-Sphere Models: Explaining Side-Chain Dihedral Angle Distributions of Thr and Val. Biophysical Journal 2012, 102: 2345-2352. PMID: 22677388, PMCID: PMC3353012, DOI: 10.1016/j.bpj.2012.01.061.Peer-Reviewed Original Research
2008
Non-random-coil Behavior as a Consequence of Extensive PPII Structure in the Denatured State
Cortajarena AL, Lois G, Sherman E, O'Hern CS, Regan L, Haran G. Non-random-coil Behavior as a Consequence of Extensive PPII Structure in the Denatured State. Journal Of Molecular Biology 2008, 382: 203-212. PMID: 18644382, PMCID: PMC2603145, DOI: 10.1016/j.jmb.2008.07.005.Peer-Reviewed Original ResearchConceptsPolyproline II helical structureRandom coil polymersKinetics of foldingAggregation diseasesFluorescence correlation spectroscopyRepeat proteinsUnfolded proteinsResidual structureCoil polymersNonnative structuresSimple polymer modelIdentical domainsPolyproline IIPolypeptide chainPPII structureCorrelation spectroscopyUnfolded stateProteinHelical structureRandom-coil statisticsDenatured statePolymer modelUnforeseen potentialCoil behaviorMisfolding