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Structure of DNA complexes with chromosomal protein HMGB1 and histone H1 in the presence of manganese ions: 2. Vibrational circular dichroism spectroscopy. / Polyanichko, A.M.; Vorob'ev, V.I.; Chikhirzhina, E.V.

In: Molecular Biology, Vol. 47, No. 2, 2013, p. 299-306.

Research output: Contribution to journal › Article › peer-review

Harvard

Polyanichko, AM, Vorob'ev, VI & Chikhirzhina, EV 2013, 'Structure of DNA complexes with chromosomal protein HMGB1 and histone H1 in the presence of manganese ions: 2. Vibrational circular dichroism spectroscopy', Molecular Biology, vol. 47, no. 2, pp. 299-306. https://doi.org/10.1134/S0026893313020118

APA

Polyanichko, A. M., Vorob'ev, V. I., & Chikhirzhina, E. V. (2013). Structure of DNA complexes with chromosomal protein HMGB1 and histone H1 in the presence of manganese ions: 2. Vibrational circular dichroism spectroscopy. Molecular Biology, 47(2), 299-306. https://doi.org/10.1134/S0026893313020118

Vancouver

Polyanichko AM, Vorob'ev VI, Chikhirzhina EV. Structure of DNA complexes with chromosomal protein HMGB1 and histone H1 in the presence of manganese ions: 2. Vibrational circular dichroism spectroscopy. Molecular Biology. 2013;47(2):299-306. https://doi.org/10.1134/S0026893313020118

Author

Polyanichko, A.M. ; Vorob'ev, V.I. ; Chikhirzhina, E.V. / Structure of DNA complexes with chromosomal protein HMGB1 and histone H1 in the presence of manganese ions: 2. Vibrational circular dichroism spectroscopy. In: Molecular Biology. 2013 ; Vol. 47, No. 2. pp. 299-306.

BibTeX

@article{24024e6299f54a9784afcc1a69efb529,
title = "Structure of DNA complexes with chromosomal protein HMGB1 and histone H1 in the presence of manganese ions: 2. Vibrational circular dichroism spectroscopy",
abstract = "DNA complexes with nonhistone HMGB1 chromatin protein and histone H1 in the presence of manganese ions were studied using methods of absorption and circular dichroism spectroscopy in the infrared region. It was demonstrated that the method provides good results, even for solutions that contain large particles, which cause scattering in UV region. It was determined that manganese ions in the complex are able to coordinate not only to different chemical groups in DNA, but also to dicarboxylic acid residues of the HMGB1 protein, which stimulates DNA condensation and slightly weakens DNA-protein interactions in the complex. {\textcopyright} 2013 Pleiades Publishing, Ltd.",
author = "A.M. Polyanichko and V.I. Vorob'ev and E.V. Chikhirzhina",
year = "2013",
doi = "10.1134/S0026893313020118",
language = "English",
volume = "47",
pages = "299--306",
journal = "Molecular Biology",
issn = "0026-8933",
publisher = "Pleiades Publishing",
number = "2",

}

RIS

TY - JOUR

T1 - Structure of DNA complexes with chromosomal protein HMGB1 and histone H1 in the presence of manganese ions: 2. Vibrational circular dichroism spectroscopy

AU - Polyanichko, A.M.

AU - Vorob'ev, V.I.

AU - Chikhirzhina, E.V.

PY - 2013

Y1 - 2013

N2 - DNA complexes with nonhistone HMGB1 chromatin protein and histone H1 in the presence of manganese ions were studied using methods of absorption and circular dichroism spectroscopy in the infrared region. It was demonstrated that the method provides good results, even for solutions that contain large particles, which cause scattering in UV region. It was determined that manganese ions in the complex are able to coordinate not only to different chemical groups in DNA, but also to dicarboxylic acid residues of the HMGB1 protein, which stimulates DNA condensation and slightly weakens DNA-protein interactions in the complex. © 2013 Pleiades Publishing, Ltd.

AB - DNA complexes with nonhistone HMGB1 chromatin protein and histone H1 in the presence of manganese ions were studied using methods of absorption and circular dichroism spectroscopy in the infrared region. It was demonstrated that the method provides good results, even for solutions that contain large particles, which cause scattering in UV region. It was determined that manganese ions in the complex are able to coordinate not only to different chemical groups in DNA, but also to dicarboxylic acid residues of the HMGB1 protein, which stimulates DNA condensation and slightly weakens DNA-protein interactions in the complex. © 2013 Pleiades Publishing, Ltd.

U2 - 10.1134/S0026893313020118

DO - 10.1134/S0026893313020118

M3 - Article

VL - 47

SP - 299

EP - 306

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 2

ER -

ID: 5700745