2013
Thermal Stability of Rhodopsin and Progression of Retinitis Pigmentosa
Liu MY, Liu J, Mehrotra D, Liu Y, Guo Y, Baldera-Aguayo PA, Mooney VL, Nour AM, Yan EC. Thermal Stability of Rhodopsin and Progression of Retinitis Pigmentosa. Journal Of Biological Chemistry 2013, 288: 17698-17712. PMID: 23625926, PMCID: PMC3682570, DOI: 10.1074/jbc.m112.397257.Peer-Reviewed Original ResearchCalcium-Dependent Ligand Binding and G‑protein Signaling of Family B GPCR Parathyroid Hormone 1 Receptor Purified in Nanodiscs
Mitra N, Liu Y, Liu J, Serebryany E, Mooney V, DeVree BT, Sunahara RK, Yan EC. Calcium-Dependent Ligand Binding and G‑protein Signaling of Family B GPCR Parathyroid Hormone 1 Receptor Purified in Nanodiscs. ACS Chemical Biology 2013, 8: 617-625. PMID: 23237450, PMCID: PMC4015634, DOI: 10.1021/cb300466n.Peer-Reviewed Original Research
2011
Artificial membrane-like environments for in vitro studies of purified G-protein coupled receptors
Serebryany E, Zhu GA, Yan EC. Artificial membrane-like environments for in vitro studies of purified G-protein coupled receptors. Biochimica Et Biophysica Acta 2011, 1818: 225-233. PMID: 21851807, DOI: 10.1016/j.bbamem.2011.07.047.Peer-Reviewed Original ResearchConceptsFunctional reconstitutionG proteinsMembrane protein structuresNative-like environmentSeven-transmembrane G-proteinMembrane-like environmentTransmembrane proteinLipidic cubic phaseCell signalingPlanar lipid membranesProtein structureMembrane mimicsMolecular levelGPCR researchLipid vesiclesLipid membranesMembraneReceptorsReconstitutionUse of micellesGPCRsSignalingNanodiscsProteinVesiclesChiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces
Fu L, Liu J, Yan EC. Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces. Journal Of The American Chemical Society 2011, 133: 8094-8097. PMID: 21534603, DOI: 10.1021/ja201575e.Peer-Reviewed Original ResearchConceptsChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyFrequency generation spectroscopyProtein secondary structureVibrational signaturesGeneration spectroscopyChiral SFG spectroscopyChiral SFG spectraRandom coilSecondary structureΑ-helixΒ-sheetLipid-water interfaceSFG spectroscopyHuman islet amyloidPeptide backboneSFG spectraH stretchAmide IReal-time characterizationSpectroscopyProtein conformationIslet amyloidStructureSitu
2010
In Situ Misfolding of Human Islet Amyloid Polypeptide at Interfaces Probed by Vibrational Sum Frequency Generation
Fu L, Ma G, Yan EC. In Situ Misfolding of Human Islet Amyloid Polypeptide at Interfaces Probed by Vibrational Sum Frequency Generation. Journal Of The American Chemical Society 2010, 132: 5405-5412. PMID: 20337445, DOI: 10.1021/ja909546b.Peer-Reviewed Original ResearchConceptsChiral optical responseSum-frequency generationCharacteristic optical propertiesSum frequency generation spectroscopyVibrational sum frequency generationAir/water interfaceFrequency generationOptical propertiesFrequency generation spectroscopyPolarization settingsGeneration spectroscopyWater interfaceInterface ProbedChiral structureStretch frequencyParallel beta-sheet structure