Joel Butterwick, PhD
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Pharmacology
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Assistant Professor of Pharmacology
Biography
Joel obtained his undergraduate degree from the University of Alberta, Canada, and his Ph.D. from Columbia University. He received postdoctoral training in the MacKinnon and Ruta Laboratories at The Rockefeller University before joining the Department of Pharmacology at Yale in 2020. As a postdoc, Joel used single-particle cryo-electron microscopy to determine the first high-resolution structure of an olfactory receptor, the insect Orco. At Yale, Joel is continuing to study smell and taste receptors to elucidate the elementary principles of chemosensory detection.
Appointments
Pharmacology
Assistant ProfessorPrimary
Other Departments & Organizations
Education & Training
- Research Associate
- The Rockefeller University (2020)
- Postdoctoral Associate
- The Rockefeller University (2014)
- PhD
- Columbia University, Biochemistry & Molecular Biophysics (2006)
- BSc
- University of Alberta, Biochemistry (1999)
Research
Overview
Medical Subject Headings (MeSH)
Biochemistry; Biophysics; Cryoelectron Microscopy; Electrophysiology; Ligand-Gated Ion Channels; Pharmacology; Smell; Taste
ORCID
0000-0002-5631-7774
Research at a Glance
Yale Co-Authors
Frequent collaborators of Joel Butterwick's published research.
Publications Timeline
A big-picture view of Joel Butterwick's research output by year.
Research Interests
Research topics Joel Butterwick is interested in exploring.
Carlos Chacon Cordon
9Publications
693Citations
Cryoelectron Microscopy
Publications
Featured Publications
Cryo-EM structure of the insect olfactory receptor Orco
Butterwick JA, del Mármol J, Kim KH, Kahlson MA, Rogow JA, Walz T, Ruta V. Cryo-EM structure of the insect olfactory receptor Orco. Nature 2018, 560: 447-452. PMID: 30111839, PMCID: PMC6129982, DOI: 10.1038/s41586-018-0420-8.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsAnchor domainOdorant receptorsSingle-particle cryo-electron microscopy structureCryo-electron microscopy structureMinimal sequence conservationReceptor familyRemarkable sequence diversityCryo-EM structureInter-subunit interactionsMicroscopy structureSequence conservationSequence diversityÅ resolutionCentral poreStructural insightsIon channelsOrcoSuch diversityOlfactory systemDiversityEnormous varietyOdor tuningFamilyInsectsSubunitsThe molecular basis of sugar detection by an insect taste receptor
Gomes J, Singh-Bhagania S, Cenci M, Chacon Cordon C, Singh M, Butterwick J. The molecular basis of sugar detection by an insect taste receptor. Nature 2024, 629: 228-234. PMID: 38447670, PMCID: PMC11062906, DOI: 10.1038/s41586-024-07255-w.Peer-Reviewed Original ResearchCitationsAltmetricConceptsLigand-binding pocketGustatory receptorsD-fructoseMolecular basisStructure-guided mutagenesisSilkworm Bombyx moriPatterns of chemical groupsIon conductivitySugar selectivityAllosteric pathwaysBombyx moriExperimental binding assaysReceptor-ligand interactionsL-sorboseComputational dockingAromatic residuesActive ligandsAllosteric couplingConformational changesSugar detectionBinding assaysFunctional assaysChemical specificityChemical groupsTaste receptors
2014
Conformational Preferences Underlying Reduced Activity of a Thermophilic Ribonuclease H
Stafford KA, Trbovic N, Butterwick JA, Abel R, Friesner RA, Palmer AG. Conformational Preferences Underlying Reduced Activity of a Thermophilic Ribonuclease H. Journal Of Molecular Biology 2014, 427: 853-866. PMID: 25550198, PMCID: PMC4349505, DOI: 10.1016/j.jmb.2014.11.023.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsAmino Acid SequenceBinding SitesCrystallography, X-RayEscherichia coliHot TemperatureHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular Dynamics SimulationMutationNuclear Magnetic Resonance, BiomolecularPrincipal Component AnalysisProtein BindingProtein ConformationRibonuclease HThermodynamicsThermus thermophilusConceptsE. coli homologWild-type proteinRibonuclease HE. coli mutantsGlycine-rich regionMesophilic homologsThermophilus enzymeColi mutantsSubstrate bindingThermophilic proteinsImportant residuesThermus thermophilusConformational dynamicsGlycine residueMesophilic enzymesActive conformationLoop regionAtom MD simulationsConformational basisReduced activityEscherichia coliHomologProteinPosition 80MD simulationsPhosphatidic acid modulation of Kv channel voltage sensor function
Hite RK, Butterwick JA, MacKinnon R. Phosphatidic acid modulation of Kv channel voltage sensor function. ELife 2014, 3: e04366. PMID: 25285449, PMCID: PMC4212207, DOI: 10.7554/elife.04366.Peer-Reviewed Original ResearchCitationsAltmetric
2010
Solution Structure and Phospholipid Interactions of the Isolated Voltage-Sensor Domain from KvAP
Butterwick JA, MacKinnon R. Solution Structure and Phospholipid Interactions of the Isolated Voltage-Sensor Domain from KvAP. Journal Of Molecular Biology 2010, 403: 591-606. PMID: 20851706, PMCID: PMC2971526, DOI: 10.1016/j.jmb.2010.09.012.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsNuclear Overhauser effect spectroscopyNuclear magnetic resonance spectroscopySolution structureIsolated voltage-sensor domainBilayer-forming lipidsMagnetic resonance spectroscopyMicelle interactionsEffect spectroscopyChemical environmentCrystal structurePhospholipid interfaceChemical propertiesResonance spectroscopyPhospholipid micellesMembrane environmentPhospholipid bilayersNanosecond timescaleMillisecond timescaleMicellesSpectroscopyAmphipathic α-helixΑ-helixVoltage sensor domainRelaxation experimentsPhysical properties
2009
Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA
Endeward B, Butterwick JA, MacKinnon R, Prisner TF. Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA. Journal Of The American Chemical Society 2009, 131: 15246-15250. PMID: 19919160, PMCID: PMC2779547, DOI: 10.1021/ja904808n.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPELDOR dataElectron-electron double resonance measurementsTransverse spin relaxation timeProbe frequencySpin relaxation timeDouble resonance measurementsChannel KcsAMagnetic field strengthSpin-label distancesCentral channel axisPELDOR experimentsDetergent-solubilized samplesField strengthRelaxation timeOscillation frequencyResonance determinationQuantitative simulationChannel axisKcsAFrequencyOrientationMeasurementsAngle
2006
An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H
Butterwick JA, Palmer AG. An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H. Protein Science 2006, 15: 2697-2707. PMID: 17088323, PMCID: PMC2242442, DOI: 10.1110/ps.062398606.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsRNase HConformational changesGly residueMesophile Escherichia coliThermophile Thermus thermophilusSolution NMR spectroscopyIntrahelical hydrogen bondsHomologous mesophilicProtein sequencesBiological functionsThermus thermophilusImportant adaptationGly insertionPutative hingeEscherichia coliRibonuclease HMesophilicResiduesDynamic processUnfavorable interactionsThermophilesThermophilicProteinNMR spectroscopyThermophilus
2005
Solution Structure of the Vts1 SAM Domain in the Presence of RNA
Edwards TA, Butterwick JA, Zeng L, Gupta YK, Wang X, Wharton RP, Palmer AG, Aggarwal AK. Solution Structure of the Vts1 SAM Domain in the Presence of RNA. Journal Of Molecular Biology 2005, 356: 1065-1072. PMID: 16405996, DOI: 10.1016/j.jmb.2005.12.004.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsSAM domainStructural basisCore helicesMultidimensional heteronuclear NMR spectroscopyRNA-binding surfaceSolution structureChemical shift perturbationsSpecific target RNAHeteronuclear NMR spectroscopyPresence of RNARNA bindingRNA recognitionC-terminusShift perturbationsTarget RNAShort helixMutational dataRNAHelix
2004
Multiple Time Scale Backbone Dynamics of Homologous Thermophilic and Mesophilic Ribonuclease HI Enzymes
Butterwick JA, Loria JP, Astrof NS, Kroenke CD, Cole R, Rance M, Palmer AG. Multiple Time Scale Backbone Dynamics of Homologous Thermophilic and Mesophilic Ribonuclease HI Enzymes. Journal Of Molecular Biology 2004, 339: 855-871. PMID: 15165855, DOI: 10.1016/j.jmb.2004.03.055.Peer-Reviewed Original ResearchCitationsAltmetric
Academic Achievements and Community Involvement
honor Whitehall Foundation Research Grant
National AwardWhitehall FoundationDetails09/01/2022United States
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Dr. Butterwick's Office
Academic Office
Sterling Hall of Medicine, B-Wing
333 Cedar Street, Ste SHM B326C
New Haven, CT 06510
Butterwick Lab
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Sterling Hall of Medicine, B-Wing
333 Cedar Street, Ste SHM B334
New Haven, CT 06510
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