Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes

Standard

Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes. / Чихиржина, Елена Всеволодовна ; Поляничко, Александр Михайлович.

в: Biophysics, Том 68, № 5, 07.03.2024, стр. 725-730.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

BibTeX

@article{29996b8a261a46b18a700c999c76afe1,

title = "Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes",

abstract = "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.",

keywords = "FTIR spectroscopy, circular dichroism, linker histone Н1, nonhistone chromosomal protein HMGB1",

author = "Чихиржина, {Елена Всеволодовна} and Поляничко, {Александр Михайлович}",

year = "2024",

month = mar,

day = "7",

doi = "10.1134/s0006350923050081",

language = "English",

volume = "68",

pages = "725--730",

journal = "Biophysics (Russian Federation)",

issn = "0006-3509",

publisher = "Springer Nature",

number = "5",

}

RIS

TY - JOUR

T1 - Analysis of the Secondary Structure of Chromatin Linker Proteins HMGB1 and H1 and their Complexes

AU - Чихиржина, Елена Всеволодовна

AU - Поляничко, Александр Михайлович

PY - 2024/3/7

Y1 - 2024/3/7

N2 - 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.

AB - 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.

KW - FTIR spectroscopy

KW - circular dichroism

KW - linker histone Н1

KW - nonhistone chromosomal protein HMGB1

UR - https://www.mendeley.com/catalogue/e5461d17-9455-3bce-a659-fa961fee1ffb/

U2 - 10.1134/s0006350923050081

DO - 10.1134/s0006350923050081

M3 - Article

VL - 68

SP - 725

EP - 730

JO - Biophysics (Russian Federation)

JF - Biophysics (Russian Federation)

SN - 0006-3509

IS - 5

ER -

ID: 117123203