{"title":"蛋白质的稳定性、热稳定性和热敏性:热力学考虑。","authors":"T Keleti","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The heat sensitivity and stability of a protein should be characterized by the Arrhenius parameters of the irreversible denaturation. The terms \"thermostability\" or \"activation enthalpy\" and \"activation entropy\" of denaturation as \"thermodynamic parameters of protein stability\" are misleading. The terms \"measure of heat sensitivity\" and \"measure of stability\" should be used as comparative data for protein structure.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Stability, heat stability and heat sensitivity of proteins: thermodynamic considerations.\",\"authors\":\"T Keleti\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The heat sensitivity and stability of a protein should be characterized by the Arrhenius parameters of the irreversible denaturation. The terms \\\"thermostability\\\" or \\\"activation enthalpy\\\" and \\\"activation entropy\\\" of denaturation as \\\"thermodynamic parameters of protein stability\\\" are misleading. The terms \\\"measure of heat sensitivity\\\" and \\\"measure of stability\\\" should be used as comparative data for protein structure.</p>\",\"PeriodicalId\":7308,\"journal\":{\"name\":\"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1985-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Stability, heat stability and heat sensitivity of proteins: thermodynamic considerations.
The heat sensitivity and stability of a protein should be characterized by the Arrhenius parameters of the irreversible denaturation. The terms "thermostability" or "activation enthalpy" and "activation entropy" of denaturation as "thermodynamic parameters of protein stability" are misleading. The terms "measure of heat sensitivity" and "measure of stability" should be used as comparative data for protein structure.