{"title":"变构蛋白:从血红蛋白中间体中吸取的教训。","authors":"Michele Perrella, Rosaria Russo","doi":"10.1152/nips.01451.2003","DOIUrl":null,"url":null,"abstract":"<p><p>Allosteric proteins, such as hemoglobin, are assemblies of functional units, which undergo quaternary structural transitions in response to concentration changes of a specific ligand. Functional properties of hemoglobin ligation intermediates indicate that the tertiary structural changes induced by the ligand do not promote an equilibrium of quaternary structures.</p>","PeriodicalId":82140,"journal":{"name":"News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society","volume":"18 ","pages":"232-6"},"PeriodicalIF":0.0000,"publicationDate":"2003-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1152/nips.01451.2003","citationCount":"6","resultStr":"{\"title\":\"Allosteric proteins: lessons to be learned from the hemoglobin intermediates.\",\"authors\":\"Michele Perrella, Rosaria Russo\",\"doi\":\"10.1152/nips.01451.2003\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Allosteric proteins, such as hemoglobin, are assemblies of functional units, which undergo quaternary structural transitions in response to concentration changes of a specific ligand. Functional properties of hemoglobin ligation intermediates indicate that the tertiary structural changes induced by the ligand do not promote an equilibrium of quaternary structures.</p>\",\"PeriodicalId\":82140,\"journal\":{\"name\":\"News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society\",\"volume\":\"18 \",\"pages\":\"232-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2003-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1152/nips.01451.2003\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1152/nips.01451.2003\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"News in physiological sciences : an international journal of physiology produced jointly by the International Union of Physiological Sciences and the American Physiological Society","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1152/nips.01451.2003","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Allosteric proteins: lessons to be learned from the hemoglobin intermediates.
Allosteric proteins, such as hemoglobin, are assemblies of functional units, which undergo quaternary structural transitions in response to concentration changes of a specific ligand. Functional properties of hemoglobin ligation intermediates indicate that the tertiary structural changes induced by the ligand do not promote an equilibrium of quaternary structures.
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