2025
Unbiased clustering of residues undergoing synchronous motions in proteins using NMR spin relaxation data
Manu V, Melacini G, Kovrigin E, Loria J, Veglia G. Unbiased clustering of residues undergoing synchronous motions in proteins using NMR spin relaxation data. Biophysical Chemistry 2025, 320: 107411. PMID: 39983456, DOI: 10.1016/j.bpc.2025.107411.Peer-Reviewed Original ResearchConceptsCluster of residuesCarr-Purcell-Meiboom-GillMicrosecond to millisecond rangeSide chain methyl groupsNMR spin relaxation dataNMR relaxation dispersionRelaxation dispersion dataSpin relaxation dataLigand bindingBackbone amidesMethyl groupPairs of residuesCAMP-dependent protein kinase ARelaxation dispersionSelection of residuesMovement of residuesActive siteNMRMacromolecular motionsRelaxation dataEnzyme catalysisProtein kinase ARibonuclease ANucleotide bindingCatalytic subunit
2017
Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions
He L, Steinocher H, Shelar A, Cohen EB, Heim EN, Kragelund BB, Grigoryan G, DiMaio D. Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions. ELife 2017, 6: e27701. PMID: 28869036, PMCID: PMC5597333, DOI: 10.7554/elife.27701.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsErythropoietin receptorTransmembrane proteinTransmembrane protein-protein interactionsTMD interactionsModel transmembrane proteinMouse erythropoietin receptorHuman erythropoietin receptorSingle methyl groupGrowth factor independenceSide chain methyl groupsCellular processesMouse cellsFactor independenceChain methyl groupsIntrinsic specificityToggle switchTraptamersMethyl groupProteinReceptor activitySpecific positionsReceptorsSpecificityOligomerization
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