2024
Identifying the minimal sets of distance restraints for FRET‐assisted protein structural modeling
Liu Z, Grigas A, Sumner J, Knab E, Davis C, O'Hern C. Identifying the minimal sets of distance restraints for FRET‐assisted protein structural modeling. Protein Science 2024, 33: e5219. PMID: 39548730, PMCID: PMC11568256, DOI: 10.1002/pro.5219.Peer-Reviewed Original ResearchMeSH KeywordsFluorescence Resonance Energy TransferMolecular Dynamics SimulationProtein ConformationProteinsConceptsForster resonance energy transferProtein structure determination techniquesCellular environmentProtein structure modelingAmino acid pairsConformational changesProteins in vivoForster resonance energy transfer studiesCrowded cellular environmentStructure determination techniquesDynamics in vivoStructures in vivoInduce conformational changesProtein structureResonance energy transferRoot-mean-square deviationAcid pairsInter-residue restraintsStructural ensemblesAmino acidsNon-physiological environmentsProteinDistance restraintsNucleic acidsAmino
2018
A threonine zipper that mediates protein–protein interactions: Structure and prediction
Oi C, Treado JD, Levine ZA, Lim CS, Knecht KM, Xiong Y, O'Hern CS, Regan L. A threonine zipper that mediates protein–protein interactions: Structure and prediction. Protein Science 2018, 27: 1969-1977. PMID: 30198622, PMCID: PMC6201716, DOI: 10.1002/pro.3505.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsProtein-protein interfacesZipper structureBeta-barrel proteinsIntermonomer hydrogen bondsBarrel proteinsThr residueSide-chain dihedral anglesBiotechnological applicationsProtein interfacesMolecular dynamics simulationsDihedral angleSide-chain conformationsThrH-bondingHydrogen bondsChain conformationMD simulationsSteric constraintsDrug discoveryDynamics simulationsResidues
2015
Equilibrium transitions between side‐chain conformations in leucine and isoleucine
Caballero D, Smith WW, O'Hern CS, Regan L. Equilibrium transitions between side‐chain conformations in leucine and isoleucine. Proteins Structure Function And Bioinformatics 2015, 83: 1488-1499. PMID: 26018846, DOI: 10.1002/prot.24837.Peer-Reviewed Original Research
2014
Connection between the packing efficiency of binary hard spheres and the glass-forming ability of bulk metallic glasses
Zhang K, Smith WW, Wang M, Liu Y, Schroers J, Shattuck MD, O'Hern CS. Connection between the packing efficiency of binary hard spheres and the glass-forming ability of bulk metallic glasses. Physical Review E 2014, 90: 032311. PMID: 25314450, DOI: 10.1103/physreve.90.032311.Peer-Reviewed Original ResearchIntrinsic 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