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12223345?677/7888101010111111zycnzj.com/://@iupui.edu))zycnzj.com/://[1]ThesmallestURFs(URFA6L),a207-nucleotide(nt)readingframeoverlappingoutofphasetheNH2-terminalportionoftheadenosinetriphosphatase(ATPase)subinit6genehasbeenidentifiedastheanimalequivalentoftherecentlydiscoveredyeastH+-ATPasesubunit8gene.zycnzj.com/://[1]ThesmallestoftheURFsisURFA6L,a207-nucleotide(nt)readingframeoverlappingoutofphasetheNH2-terminalportionoftheadenosinetriphosphatase(ATPase)subinit6Gene;ithasbeenidentifiedastheanimalequivalentoftherecentlydiscoveredyeastH+-ATPasesubunit8gene.3.[1]URFA6LhasbeenidentifiedastheanimalequivalentoftherecentlydiscoveredyeastH+-ATPasesubunit8gene.RecentlydiscoveredyeastH+-ATPasesubunit8genehasacorrespondinganimalequivalentgeneURFA6L.[1]Theenthalpyofhydrogenbondformationbetweenthenucleosidebases2-deoxyguanosine(dG)and2-deoxycytidine(dC)hasbeendeterminedbydirectmeasurement.directmeasurement[1]Wehavedirectlymeasuredtheenthalpyofhydrogenbondformationbetweenthenucleosidebases2-deoxyguanosine(dG)and2-deoxycytidine(dC).[1]Theenthalpyofhydrogenbondformationbetweenthenucleosidebases2-deoxyguanosine(dG)and2-deoxycytidine(dC)hasbeendeterminedbydirectmeasurement.dGanddCwerederivatizedatthe5and3hydroxylswithtriisopropylsilylgroupstoobtainsolubilityofthenucleosidesinnon-aqueoussolventsandtopreventtheribosehydroxylsfromforminghydrogenbonds.Fromisoperibolictitrationmeasurements,theenthalpyofdC:dGbasepairformationis-6.650.32kcal/mol.(enthalpy)[1]zycnzj.com/://(dG)and2-deoxycytidine(dC).dGanddCwerederivatizedatthe5and3hydroxylswithtriisopropylsilylgroups;thesegroupsservebothtosolubilizethenucleosidesinnon-aqueoussolventsandtopreventtheribosehydroxylsfromforminghydrogenbonds.TheenthalpyofdC:dGbasepairformationis-6.650.32kcal/molaccordingtoisoperibolictitrationmeasurements,1dGdC2[1]Largeearthquakesalongagivenfaultsegmentdonotoccuratrandomintervalsbecauseittakestimetoaccumulatethestrainenergyfortherupture.Theratesatwhichtectonicplatesmoveandaccumulatestrainattheirboundariesareapproximatelyuniform.Therefore,infirstapproximation,onemayexpectthatlargerupturesofthesamefaultsegmentwilloccuratapproximatelyconstanttimeintervals.Ifsubsequentmainshockshavedifferentamountsofslipacrossthefault,thentherecurrencetimemayvary,andthebasicideaofperiodicmainshocksmustbemodified.RateOfStrainAccumulation)[1]Largeearthquakesalongagivenfaultsegmentdonotoccuratrandomintervalsbecauseittakestimetoaccumulatethestrainenergyfortherupture.Theratesofstrainaccumulationattheboundariesoftectonicplatesareapproximatelyuniform.Therefore,nearlyconstanttimeintervals(atfirstapproximation)wouldbeexpectedbetweenlargerupturesofthesamefaultsegment.[However?],therecurrencetimemayvary;thebasicideaofperiodicmainshocksmayneedtobemodifiedifsubsequentmainshockshavedifferentamountsofslipacrossthefault.!12:[1]2:[1]Temp(°C)Time25027329632123215TimeTemp(°C)02532762912321532zycnzj.com/://:BenchmarkSALIGNLindahlPROSPECTOR3LiveBench8MethodAlignmentMaxSubMaxSubMaxSubSPARKS53.1%325.9529.038.3SPARKS254.9%341.0591.040.7Thiswork56.6%349.2601.942.2Helvetica)[2]XY?zycnzj.com/://).2).()3).4).()5).6)./()()/()()()1)2)zycnzj.com/://()()“Stericrestrictionsinproteinfolding:analpha-helixcannotbefollowedbyacontiguousbeta-strand”“Interpretingthefoldingkineticsofhelicalproteins”“Nativeproteinsaresurface-moltensolids:ApplicationoftheLindemanncriterionforthesolidversusliquidstate”“Nativeproteinsaresurface-moltensolids”()[3]Assessingsecondarystructureassignmentsofproteinstructuresbyusingpairwisesequence-alignmentbenchmarksThesecondarystructureofaproteinreferstothelocalconformationofitspolypeptidebackbone.Knowingsecondarystructuresofproteinsisessentialfortheirstructureclassification,understandingfoldingdynamicsandmechanisms,anddiscoveringconservedstructural/functionalmotifs.Secondarystr

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