{"title":"蛋白质-溶剂界面:一个大的飞溅","authors":"A. Purkiss, S. Skoulakis, J. Goodfellow","doi":"10.1098/rsta.2001.0863","DOIUrl":null,"url":null,"abstract":"Water plays many roles in its interaction with water–soluble proteins through hydrogen bonding, electrostatic shielding and the hydrophobic effect. Water molecules are found on the surface of proteins, in clefts and channels and in cavities buried beneath the surface. We review data on these relating to structure, thermodynamics, dynamics and function. At interfaces, water may play two roles. Firstly, the absence of solvent may contribute to the favourable free energy of binding. Secondly, the presence of solvent may control the level of specificity or contribute to a favourable enthalpy. Finally, we review the role of solvent in unfolding proteins and the relation of protein unfolding/misfolding to disease.","PeriodicalId":20023,"journal":{"name":"Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2001-08-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"21","resultStr":"{\"title\":\"The protein–solvent interface: a big splash\",\"authors\":\"A. Purkiss, S. Skoulakis, J. Goodfellow\",\"doi\":\"10.1098/rsta.2001.0863\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Water plays many roles in its interaction with water–soluble proteins through hydrogen bonding, electrostatic shielding and the hydrophobic effect. Water molecules are found on the surface of proteins, in clefts and channels and in cavities buried beneath the surface. We review data on these relating to structure, thermodynamics, dynamics and function. At interfaces, water may play two roles. Firstly, the absence of solvent may contribute to the favourable free energy of binding. Secondly, the presence of solvent may control the level of specificity or contribute to a favourable enthalpy. Finally, we review the role of solvent in unfolding proteins and the relation of protein unfolding/misfolding to disease.\",\"PeriodicalId\":20023,\"journal\":{\"name\":\"Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2001-08-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"21\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1098/rsta.2001.0863\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1098/rsta.2001.0863","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Water plays many roles in its interaction with water–soluble proteins through hydrogen bonding, electrostatic shielding and the hydrophobic effect. Water molecules are found on the surface of proteins, in clefts and channels and in cavities buried beneath the surface. We review data on these relating to structure, thermodynamics, dynamics and function. At interfaces, water may play two roles. Firstly, the absence of solvent may contribute to the favourable free energy of binding. Secondly, the presence of solvent may control the level of specificity or contribute to a favourable enthalpy. Finally, we review the role of solvent in unfolding proteins and the relation of protein unfolding/misfolding to disease.
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