{"title":"本质无序蛋白质动力学中的静电和疏水性","authors":"Renee Vancraenenbroeck, Hagen Hofmann","doi":"10.1140/epje/s10189-023-00383-7","DOIUrl":null,"url":null,"abstract":"<div><p>Internal friction is a major contribution to the dynamics of intrinsically disordered proteins (IDPs). Yet, the molecular origin of internal friction has so far been elusive. Here, we investigate whether attractive electrostatic interactions in IDPs modulate internal friction differently than the hydrophobic effect. To this end, we used nanosecond fluorescence correlation spectroscopy (nsFCS) and single-molecule Förster resonance energy transfer (FRET) to quantify the conformation and dynamics of the disordered DNA-binding domains Myc, Max and Mad at different salt concentrations. We find that internal friction effects are stronger when the chain is compacted by electrostatic attractions compared to the hydrophobic effect. Although the effect is moderate, the results show that the heteropolymeric nature of IDPs is reflected in their dynamics.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":790,"journal":{"name":"The European Physical Journal E","volume":"46 12","pages":""},"PeriodicalIF":1.8000,"publicationDate":"2023-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1140/epje/s10189-023-00383-7.pdf","citationCount":"0","resultStr":"{\"title\":\"Electrostatics and hydrophobicity in the dynamics of intrinsically disordered proteins\",\"authors\":\"Renee Vancraenenbroeck, Hagen Hofmann\",\"doi\":\"10.1140/epje/s10189-023-00383-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Internal friction is a major contribution to the dynamics of intrinsically disordered proteins (IDPs). Yet, the molecular origin of internal friction has so far been elusive. Here, we investigate whether attractive electrostatic interactions in IDPs modulate internal friction differently than the hydrophobic effect. To this end, we used nanosecond fluorescence correlation spectroscopy (nsFCS) and single-molecule Förster resonance energy transfer (FRET) to quantify the conformation and dynamics of the disordered DNA-binding domains Myc, Max and Mad at different salt concentrations. We find that internal friction effects are stronger when the chain is compacted by electrostatic attractions compared to the hydrophobic effect. Although the effect is moderate, the results show that the heteropolymeric nature of IDPs is reflected in their dynamics.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>\",\"PeriodicalId\":790,\"journal\":{\"name\":\"The European Physical Journal E\",\"volume\":\"46 12\",\"pages\":\"\"},\"PeriodicalIF\":1.8000,\"publicationDate\":\"2023-12-21\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://link.springer.com/content/pdf/10.1140/epje/s10189-023-00383-7.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The European Physical Journal E\",\"FirstCategoryId\":\"4\",\"ListUrlMain\":\"https://link.springer.com/article/10.1140/epje/s10189-023-00383-7\",\"RegionNum\":4,\"RegionCategory\":\"物理与天体物理\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The European Physical Journal E","FirstCategoryId":"4","ListUrlMain":"https://link.springer.com/article/10.1140/epje/s10189-023-00383-7","RegionNum":4,"RegionCategory":"物理与天体物理","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
Electrostatics and hydrophobicity in the dynamics of intrinsically disordered proteins
Internal friction is a major contribution to the dynamics of intrinsically disordered proteins (IDPs). Yet, the molecular origin of internal friction has so far been elusive. Here, we investigate whether attractive electrostatic interactions in IDPs modulate internal friction differently than the hydrophobic effect. To this end, we used nanosecond fluorescence correlation spectroscopy (nsFCS) and single-molecule Förster resonance energy transfer (FRET) to quantify the conformation and dynamics of the disordered DNA-binding domains Myc, Max and Mad at different salt concentrations. We find that internal friction effects are stronger when the chain is compacted by electrostatic attractions compared to the hydrophobic effect. Although the effect is moderate, the results show that the heteropolymeric nature of IDPs is reflected in their dynamics.
期刊介绍：
EPJ E publishes papers describing advances in the understanding of physical aspects of Soft, Liquid and Living Systems.
Soft matter is a generic term for a large group of condensed, often heterogeneous systems -- often also called complex fluids -- that display a large response to weak external perturbations and that possess properties governed by slow internal dynamics.
Flowing matter refers to all systems that can actually flow, from simple to multiphase liquids, from foams to granular matter.
Living matter concerns the new physics that emerges from novel insights into the properties and behaviours of living systems. Furthermore, it aims at developing new concepts and quantitative approaches for the study of biological phenomena. Approaches from soft matter physics and statistical physics play a key role in this research.
The journal includes reports of experimental, computational and theoretical studies and appeals to the broad interdisciplinary communities including physics, chemistry, biology, mathematics and materials science.
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