1、F794780中圖分類碼：Q61，Q5182專業(yè)分類碼：081704學科分類代碼：1807130天津理工大學碩士學位論文蛋白質折疊，結構拆解和結合部位多樣性的研究(申請碩士學位)學科專業(yè)：應用化學研究方向：生物信息學研究生：田晶指導教師：黃積濤教授二零零五年一月Studiesofproteinfoldingmechanism，structuralsplittingandbindingsitediversityAbstractTherea

2、rethreeinformationsoarcesofproteinscienceinbioinformatics：sequence，structureandfunction111eproblemofproteinfoldingbelongstotherelationshipbetweenproteinsequenceanditsstructure；andtheproblemofrelationshipbetweenproteinstr

3、uctureanditsbiologicalfunctionaleoneofthelargestchallengesinmolecularbiologyStructuraldeterminantsofproteinfoldingmechanismwerestudiedWeassumedthatthereisarepulsivepotentialbetweenaminoacidresiduepairsinproteinstructureW

4、henproteinfolds，theirconformationcollapsesAresidueliesclosetoanotherresidueandSOwouldcausesterichindrancetolutherfoldSothefoldingratedecreasedquicklywitllanincreasingmagnitudeoftherepulsivebarrierTwodifferentmathematical

5、formulaswcfeusedtodescribethepotentialfunetionOneisanequationbased011Lennard／onesformulawhichthepotentialiSinverselyproportionaltesiduedistancetothe65thpower(E=1，礦3、。TheotheriSsimilartoMorseformulaandthepotentialdecrease

6、dexponentiallywithincreaseinthedistance忸=e156)【d)66twostateproteinsmultistateproteinsandshortpeptidewereanalyzedstatistically11他resultshowsastrongcorrelationbetweenthepotentialsandfoldingrates，whichcorrelationeoefficiema

7、rcO80and081，t刪ve1yContactresidues趣ethedeteminantsofprotein—foldingkineticsProtein嗣nKtl∞∞，especiallytertiarystructures，arecloselyrelatedtotheirbiologicalrolesHoweveritisdifficulttodistinguishbetweensecondarystructureandte

8、rtiaryoneHere，thebackbonestructureofaproteinWassuppressedthenoiseofhi【ghfrequencyandfoldingpatternoflowfrequencyWasreserved11Iisimpliesthatsecondarystnlctureisremovedfromproteinstructureand“pure’tertiaryslructureisobtain

9、edThjsapproachhighii曲tsthelongrangestructureofproteinandCanprovideadatasourceforpredictionofproteinstructttreItisverydifficulttosuperposethespatialstructuresofproteinsinstudyoftherelationshipbetweenproteinstructuresandth

10、eirfunctionsWehereinselectedporphyrinbindingmyoglobinproteinswhicharedifferentinsequenceandstructure‰msuperpositionofglobalstructuresofproteinsWasperformedusingligandsupcrpositionStructuraldiversityofaseriesofproteinsiss