{"title":"发布信息TOC","authors":"","doi":"10.1002/cpps.81","DOIUrl":null,"url":null,"abstract":"<p><b>Cover</b>: In Wolfe et al. (https://doi.org/10.1002/cpps.96), Representative two phases of the isothermal detergent desorption of membrane proteins. (A) The initial phase is detergent predesolvation. (B) The follow-up, time-dependent phase is detergent desolvation. Predesolvation results from the dissociation of a relatively small number of detergent monomers from membrane proteins. This process is accompanied by a relatively small and slow change in the FP anisotropy with respect to the initial value, rmax. The second phase depicts a large and fast alteration in the FP anisotropy, as it is representative of the loss of many detergent monomers from membrane proteins. This major change in the average molecular mass of proteomicelles is reflected in a drastic alteration of the FP anisotropy, and occurs in a single-exponential fashion (right-hand panels). The kinetic rates of both predesolvation and desolvation phases are dependent on the final detergent concentration (Wolfe et al., 2018a). For example, the kinetic rates are greater for lower detergent concentrations in the protein sample. Reprinted with permission from reference Wolfe et al. (2018b). Copyright 2018, American Chemical Society.\n\n <figure>\n <div><picture>\n <source></source></picture><p></p>\n </div>\n </figure></p>","PeriodicalId":10866,"journal":{"name":"Current Protocols in Protein Science","volume":"97 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2019-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/cpps.81","citationCount":"0","resultStr":"{\"title\":\"Issue Information TOC\",\"authors\":\"\",\"doi\":\"10.1002/cpps.81\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><b>Cover</b>: In Wolfe et al. (https://doi.org/10.1002/cpps.96), Representative two phases of the isothermal detergent desorption of membrane proteins. (A) The initial phase is detergent predesolvation. (B) The follow-up, time-dependent phase is detergent desolvation. Predesolvation results from the dissociation of a relatively small number of detergent monomers from membrane proteins. This process is accompanied by a relatively small and slow change in the FP anisotropy with respect to the initial value, rmax. The second phase depicts a large and fast alteration in the FP anisotropy, as it is representative of the loss of many detergent monomers from membrane proteins. This major change in the average molecular mass of proteomicelles is reflected in a drastic alteration of the FP anisotropy, and occurs in a single-exponential fashion (right-hand panels). The kinetic rates of both predesolvation and desolvation phases are dependent on the final detergent concentration (Wolfe et al., 2018a). For example, the kinetic rates are greater for lower detergent concentrations in the protein sample. Reprinted with permission from reference Wolfe et al. (2018b). Copyright 2018, American Chemical Society.\\n\\n <figure>\\n <div><picture>\\n <source></source></picture><p></p>\\n </div>\\n </figure></p>\",\"PeriodicalId\":10866,\"journal\":{\"name\":\"Current Protocols in Protein Science\",\"volume\":\"97 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-09-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1002/cpps.81\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Protocols in Protein Science\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/cpps.81\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Protocols in Protein Science","FirstCategoryId":"1085","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/cpps.81","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0
摘要
封面:在Wolfe等人(https://doi.org/10.1002/cpps.96)中,有代表性的两相等温洗涤剂解吸膜蛋白。(A)初始阶段为洗涤剂预溶。(B)后续的、随时间变化的阶段是洗涤剂脱溶。预溶是由相对少量的洗涤剂单体从膜蛋白中解离而产生的。这个过程伴随着相对于初始值rmax的FP各向异性的相对较小和缓慢的变化。第二阶段描述了FP各向异性的大而快速的变化,因为它代表了膜蛋白中许多洗涤剂单体的损失。蛋白团束平均分子质量的这一重大变化反映在FP各向异性的剧烈变化中,并以单指数方式发生(右图)。预溶和脱溶相的动力学速率取决于最终洗涤剂浓度(Wolfe et al., 2018a)。例如,对于蛋白质样品中较低的洗涤剂浓度,动力学速率更大。经参考文献Wolfe et al. (2018b)许可转载。版权所有2018,美国化学会。
Cover: In Wolfe et al. (https://doi.org/10.1002/cpps.96), Representative two phases of the isothermal detergent desorption of membrane proteins. (A) The initial phase is detergent predesolvation. (B) The follow-up, time-dependent phase is detergent desolvation. Predesolvation results from the dissociation of a relatively small number of detergent monomers from membrane proteins. This process is accompanied by a relatively small and slow change in the FP anisotropy with respect to the initial value, rmax. The second phase depicts a large and fast alteration in the FP anisotropy, as it is representative of the loss of many detergent monomers from membrane proteins. This major change in the average molecular mass of proteomicelles is reflected in a drastic alteration of the FP anisotropy, and occurs in a single-exponential fashion (right-hand panels). The kinetic rates of both predesolvation and desolvation phases are dependent on the final detergent concentration (Wolfe et al., 2018a). For example, the kinetic rates are greater for lower detergent concentrations in the protein sample. Reprinted with permission from reference Wolfe et al. (2018b). Copyright 2018, American Chemical Society.
期刊介绍:
With the mapping of the human genome, more and more researchers are exploring protein structures and functions in living organisms. Current Protocols in Protein Science provides protein scientists, biochemists, molecular biologists, geneticists, and others with the first comprehensive suite of protocols for this growing field.