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