Featured Publications
Thermodynamically driven assemblies and liquid–liquid phase separations in biology
Falahati H, Haji-Akbari A. Thermodynamically driven assemblies and liquid–liquid phase separations in biology. Soft Matter 2019, 15: 1135-1154. PMID: 30672955, DOI: 10.1039/c8sm02285b.Peer-Reviewed Original ResearchConceptsPhase separationBiological self-assembly processesSelf-assembly processLiquid-liquid phase separationUnderlying physical principlesDriven AssemblyIntermolecular interactionsPhysical originBiomolecular complexesMembraneless organellesMolecular simulationsPhysicsPhysical principlesStatistical physicsSeparationThermodynamic variablesExperimental verificationAssembly processSustenance of lifeThermodynamicsBiological implicationsAssemblyComputational techniquesSubcellular structuresEnergy
2020
Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells
Benedetti L, Marvin JS, Falahati H, Guillén-Samander A, Looger LL, De Camilli P. Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells. ELife 2020, 9: e63230. PMID: 33174843, PMCID: PMC7735757, DOI: 10.7554/elife.63230.Peer-Reviewed Original ResearchConceptsProtein fusion partnersSmall subcellular volumesSubcellular optogeneticsOrganelle contactsHomodimerization interfaceProtein modulesMammalian cellsBiological processesPhysiological processesSubcellular organellesLow temperature preincubationSimultaneous photoactivationFusion partnerCell preincubationWhole cellsSubcellular volumesConcatemerizationSpatial controlSpatiotemporal confinementCellsNeurosporaOrganellesHeterodimersVIVIDProtein
2013
Transmitting the allosteric signal in methylglyoxal synthase
Falahati H, Pazhang M, Zareian S, Ghaemi N, Rofougaran R, Hofer A, Rezaie AR, Khajeh K. Transmitting the allosteric signal in methylglyoxal synthase. Protein Engineering Design And Selection 2013, 26: 445-452. PMID: 23592737, DOI: 10.1093/protein/gzt014.Peer-Reviewed Original ResearchConceptsAllosteric signalMethylglyoxal synthaseEnzyme methylglyoxal synthaseSite of phosphateActive site amino acidsSite-directed mutagenesisSite amino acidsAllosteric networkDynamic proteinsTerminal tailNew salt bridgesSer-55Gly-56Allosteric mechanismActive siteAsp-10Val-101Arg-97AllosteryThermus spAmino acidsPhosphoryl groupHomotropic allosterySalt bridgeModel system
2010
Cloning, Expression, and Characterization of a Novel Methylglyoxal Synthase from Thermus sp. Strain GH5
Pazhang M, Khajeh K, Asghari SM, Falahati H, Naderi-Manesh H. Cloning, Expression, and Characterization of a Novel Methylglyoxal Synthase from Thermus sp. Strain GH5. Applied Biochemistry And Biotechnology 2010, 162: 1519-1528. PMID: 20419481, DOI: 10.1007/s12010-010-8933-0.Peer-Reviewed Original ResearchConceptsMethylglyoxal synthaseThermus spAmino acid sequenceGel filtration experimentsAcid sequenceHexameric enzymeAllosteric inhibitorsQuaternary structureEnzyme subunitMolecular massAmino acidsArg-150GH5Q-SepharoseGenesTMGSSpEnzymeSynthasePresence of phosphateOptimum activityHill coefficientCloningSubunitsPolypeptide