Thermodynamic Properties of Linear Protein Solutions：an Application to Type Ⅰ Antifreeze Protein Solutions研究.pdfVIP

CHEM．RES．CHINESEUNIVERSITIES2012，28(6)，1070— 1073 ThermodynamicPropertiesofLinearProteinSolutions： anApplicationtoTypeIAntifreezeProteinSolutions LILi．fen，-．LIANGXi．xia andLIQian．zhong JDepartmentofPhysics，InnerMongoliaUniversity,Hohhot010021，尸R-China, 2．DepartmentofBasicCurriculum，NorthChinaInstituteofScienceandTechnology,Bejiing101601， R．China Abstract A statisticalthermodynamictheoryoflinearproteinsolutionswasproposedwiththeaidofalatticemodel andappliedtotypeIantifreezeprotein(AFPI)solutions．ThenumericalresultsforseveralAFPlsolutionsshowthat theGibbsfunctionofthesolutionhasaminimum atacertainproteinconcentration，buttheproteinchemicalpotential increaseswithincreasingtheconcentration Theinfluencesoftemperatureandproteinchain length ontheAFPI chemicalpotentialwerealsodiscussed．Theevaluation f0rthecolligativedepressionoftherfeezingpointconfirms thattheantirfeezeactionshouldberecognizedasnon．colligative．Thetheoreticaldeductionofrtheconcentrationde— pendenceofthethermalhysteresisactivitycoincidesqualitativelywiththepreviousexperimentalandtheoreticalre suits． Keywords Antirfeezeproteinsolution；Gibbsfunction；Chemicalpotential；Thermalhysteresis ArticleID 1005—9040(2012、-06-1070-04 1 IntroductiOn dynamicpropertiesofAFPsolutions．ThemoleculesoftypeI antirfeezeproteins(AFPIs)havethetypicallinearchainstruc— Antifreezeprotein(AFP、moleculescanbeadsorbedonto ture．SO the statistica1thermodynamic investigationson the thesurfacesoficecoresinthesolutionna dinhibittheirfurther propertiesof1inearprotein solutionsare invoked ofrunder— growth．so也attherfeezingtemperatureislowered without