2025
Protein Folding as a Jamming Transition
Grigas A, Liu Z, Logan J, Shattuck M, O'Hern C. Protein Folding as a Jamming Transition. PRX Life 2025, 3: 013018. PMID: 38800654, PMCID: PMC11118678, DOI: 10.1103/prxlife.3.013018.Peer-Reviewed Original Research
2024
Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel
Rostovtseva T, Weinrich M, Jacobs D, Rosencrans W, Bezrukov S. Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel. International Journal Of Molecular Sciences 2024, 25: 2204. PMID: 38396879, PMCID: PMC10889239, DOI: 10.3390/ijms25042204.Peer-Reviewed Original ResearchConceptsRegulation of protein-protein interactionsProtein-protein interactionsNon-lamellar lipidsMembrane hydrophobic coreMembrane remodelingMechanical properties of lipid bilayersMembrane bindingProperties of lipid bilayersRegulatory functionsTubulin bindingTubulinHydrophobic regionLipid headgroupsHydrophobic coreCell proliferationLipid bilayerPlanar lipid membranesMembrane mechanical propertiesMembraneMolecular probesLipid packingLipidLipid membranesGramicidin A channelBinding
2020
Using physical features of protein core packing to distinguish real proteins from decoys
Grigas AT, Mei Z, Treado JD, Levine ZA, Regan L, O'Hern CS. Using physical features of protein core packing to distinguish real proteins from decoys. Protein Science 2020, 29: 1931-1944. PMID: 32710566, PMCID: PMC7454528, DOI: 10.1002/pro.3914.Peer-Reviewed Original ResearchConceptsProtein structureReal protein structuresProtein coreReal proteinsAmino acid sequenceProtein core packingProtein structure predictionBiennial Critical AssessmentSet of decoysAcid sequenceProtein packingHydrophobic residuesCore packingStructure Prediction competitionTarget sequenceStructure predictionDecoy structuresProteinHydrophobic coreDecoysResiduesProtein Structure Prediction competitionsKey physical featuresSequenceImportant physical featuresFreezing and piercing of in vitro asymmetric plasma membrane by α-synuclein
Heo P, Pincet F. Freezing and piercing of in vitro asymmetric plasma membrane by α-synuclein. Communications Biology 2020, 3: 148. PMID: 32235856, PMCID: PMC7109109, DOI: 10.1038/s42003-020-0883-7.Peer-Reviewed Original ResearchMeSH Keywordsalpha-SynucleinCell MembraneElectric CapacitanceFluorescence Recovery After PhotobleachingHydrophobic and Hydrophilic InteractionsLab-On-A-Chip DevicesMembrane FluidityMembrane LipidsMembrane PotentialsMembranes, ArtificialMicrofluidic Analytical TechniquesNeuronsProtein AggregatesProtein Aggregation, PathologicalProtein BindingProtein ConformationStructure-Activity RelationshipSynucleinopathiesConceptsPlasma membraneMembrane-bound proteinsAccumulation of aggregatesΑ-synucleinCytosolic leafletMembrane topologyMembrane hydrophobic coreCytosolic proteinsProteinExtracellular onesHydrophobic corePathological roleDiscrete sizesMembraneLeafletsMembrane capacitanceNeurological diseasesLipidsAccumulationMicrofluidic setup
2000
Design of single-layer β-sheets without a hydrophobic core
Koide S, Huang X, Link K, Koide A, Bu Z, Engelman D. Design of single-layer β-sheets without a hydrophobic core. Nature 2000, 403: 456-460. PMID: 10667801, DOI: 10.1038/35000255.Peer-Reviewed Original ResearchConceptsSingle-layer β-sheetΒ-sheetHydrophobic coreΒ-sheet segmentsProtein foldingHydrogen-deuterium exchangeOuter surface protein AΒ-sheet structureChemical denaturationSmall-angle X-rayProtein AFoldingMain thermodynamic driving forceSurface protein ABorrelia burgdorferiNuclear magnetic resonanceThermodynamic driving forceMisfoldingNonpolar moietiesHydrophobic effectSolvent resultsProteinAdjacent unitsDenaturationVariants
1997
Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
Munson M, Anderson K, Regan L. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Structure 1997, 2: 77-87. PMID: 9080201, DOI: 10.1016/s1359-0278(97)00008-4.Peer-Reviewed Original Research
1994
Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane.
Mothes W, Prehn S, Rapoport T. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. The EMBO Journal 1994, 13: 3973-3982. PMID: 8076593, PMCID: PMC395317, DOI: 10.1002/j.1460-2075.1994.tb06713.x.Peer-Reviewed Original ResearchMeSH KeywordsAffinity LabelsAmino Acid SequenceAzirinesBenzoatesBiological TransportCell CompartmentationCross-Linking ReagentsDNA Mutational AnalysisEndoplasmic ReticulumLysineMembrane ProteinsModels, BiologicalMolecular Sequence DataProlactinProtein BiosynthesisProtein PrecursorsSEC Translocation ChannelsStructure-Activity RelationshipUltraviolet RaysConceptsSec61 alphaNascent chainsProtein interactsSignal sequenceProtein-conducting channelSecretory protein preprolactinNascent polypeptide chainsEndoplasmic reticulum membranePhoto-crosslinking approachSec61p complexER membraneMembrane proteinsMembrane environmentSecretory proteinsPolypeptide segmentsReticulum membranePolypeptide chainTranslocation processHydrophobic coreRibosomesProtein environmentProteinTranslocationPhotoreactive groupSequence
1992
Probing Protein Stability with Unnatural Amino Acids
Mendel D, Ellman J, Chang Z, Veenstra D, Kollman P, Schultz P. Probing Protein Stability with Unnatural Amino Acids. Science 1992, 256: 1798-1802. PMID: 1615324, DOI: 10.1126/science.1615324.Peer-Reviewed Original ResearchConceptsProtein stabilityUnnatural amino acid mutagenesisAmino acid mutagenesisUnnatural amino acidsSide-chain conformational entropyAmino acidsPosition 133T4 lysozymeHydrophobic coreConformational entropySpecific replacementChain conformational entropyMolecular modelingLeucineSide chain structureMutagenesisNorvalineSerineAcidStepwise removalEthylglycineProteinMethyl groupStructural changes
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