{"title":"Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes","authors":"E. V. Chikhirzhina, A. M. Polyanichko","doi":"10.1134/S0006350923050081","DOIUrl":null,"url":null,"abstract":"<p>The nonhistone chromosomal protein HMGB1 and histone H1 are chromatin linker proteins. The functions of linker proteins are closely related to their conformational state. The structure of proteins that play a key role in the formation of higher levels of chromatin structural organization is being actively studied. In this study, a comparative analysis of the secondary structure of the linker histone H1 and the nonhistone protein HMGB1 was carried out. Using circular dichroism in the UV region and FTIR spectroscopy, it was shown that positively charged histone H1 binds to the C-terminal fragment of HMGB1, stabilizing the resulting complex and inducing the formation of additional α-helical regions in both proteins.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":"68 5","pages":"725 - 730"},"PeriodicalIF":4.0330,"publicationDate":"2024-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysics","FirstCategoryId":"4","ListUrlMain":"https://link.springer.com/article/10.1134/S0006350923050081","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0
Abstract
The nonhistone chromosomal protein HMGB1 and histone H1 are chromatin linker proteins. The functions of linker proteins are closely related to their conformational state. The structure of proteins that play a key role in the formation of higher levels of chromatin structural organization is being actively studied. In this study, a comparative analysis of the secondary structure of the linker histone H1 and the nonhistone protein HMGB1 was carried out. Using circular dichroism in the UV region and FTIR spectroscopy, it was shown that positively charged histone H1 binds to the C-terminal fragment of HMGB1, stabilizing the resulting complex and inducing the formation of additional α-helical regions in both proteins.
BiophysicsBiochemistry, Genetics and Molecular Biology-Biophysics
CiteScore
1.20
自引率
0.00%
发文量
67
期刊介绍：
Biophysics is a multidisciplinary international peer reviewed journal that covers a wide scope of problems related to the main physical mechanisms of processes taking place at different organization levels in biosystems. It includes structure and dynamics of macromolecules, cells and tissues; the influence of environment; energy transformation and transfer; thermodynamics; biological motility; population dynamics and cell differentiation modeling; biomechanics and tissue rheology; nonlinear phenomena, mathematical and cybernetics modeling of complex systems; and computational biology. The journal publishes short communications devoted and review articles.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
