2016
Understanding the physical basis for the side‐chain conformational preferences of methionine
Virrueta A, O'Hern CS, Regan L. Understanding the physical basis for the side‐chain conformational preferences of methionine. Proteins Structure Function And Bioinformatics 2016, 84: 900-911. PMID: 26917446, DOI: 10.1002/prot.25026.Peer-Reviewed Original ResearchConceptsSide-chain dihedral angle distributionsAmino acidsHigh-resolution protein crystal structuresProtein-protein interfacesMet side chainsStructure of MetProtein crystal structuresVersatile amino acidDihedral angle distributionsProtein structureProtein coreIleSide chainsLeuValPheAcidThrObserved distributionCrystal structureMetSMethionineSerTyrSelenomethionine
2014
Predicting the side‐chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models
Zhou AQ, O'Hern CS, Regan L. Predicting the side‐chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models. Proteins Structure Function And Bioinformatics 2014, 82: 2574-2584. PMID: 24912976, DOI: 10.1002/prot.24621.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
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