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Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection. / Kuznetsov, Nikita A.

In: Photonics, Vol. 10, No. 9, 1033, 09.2023.

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

Harvard

Kuznetsov, NA 2023, 'Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection', Photonics, vol. 10, no. 9, 1033. https://doi.org/10.3390/photonics10091033

APA

Kuznetsov, N. A. (2023). Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection. Photonics, 10(9), [1033]. https://doi.org/10.3390/photonics10091033

Vancouver

Kuznetsov NA. Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection. Photonics. 2023 Sept;10(9):1033. doi: 10.3390/photonics10091033

Author

Kuznetsov, Nikita A. / Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection. In: Photonics. 2023 ; Vol. 10, No. 9.

BibTeX

@article{358e92b470c247d6b98837e78aaacfff,
title = "Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection",
abstract = "This review deals with modern approaches to systematic research on molecular-kinetic mechanisms of damage recognition and removal by pro- and eukaryotic enzymes of DNA base excision repair. To this end, using DNA glycosylases from different structural families as an example—as well as apurinic/apyrimidinic endonuclease, which differs structurally and catalytically from DNA glycosylases—a comprehensive methodology is described in detail regarding studies on the mechanisms of action of DNA repair enzymes in humans and in Escherichia coli. This methodology is based on kinetic, thermodynamic, and mutational analyses of alterations in the conformation of molecules of an enzyme and of DNA during their interaction in real time. The described techniques can be used to analyze any protein–protein or protein–nucleic acid interactions.",
keywords = "AP endonuclease, DNA damage, DNA glycosylase, base excision repair, catalysis, enzymatic activity, fluorescence, mechanism, mutational analysis, pre-steady-state kinetics, thermodynamics",
author = "Kuznetsov, {Nikita A.}",
note = "This work was supported by Russian Science Foundation grant No. 23-44-00064. Partial support by a Russian-State-funded budget project No. 121031300041-4 for the routine maintenance of the equipment used is also acknowledged.",
year = "2023",
month = sep,
doi = "10.3390/photonics10091033",
language = "English",
volume = "10",
journal = "Photonics",
issn = "2304-6732",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "9",

}

RIS

TY - JOUR

T1 - Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection

AU - Kuznetsov, Nikita A.

N1 - This work was supported by Russian Science Foundation grant No. 23-44-00064. Partial support by a Russian-State-funded budget project No. 121031300041-4 for the routine maintenance of the equipment used is also acknowledged.

PY - 2023/9

Y1 - 2023/9

N2 - This review deals with modern approaches to systematic research on molecular-kinetic mechanisms of damage recognition and removal by pro- and eukaryotic enzymes of DNA base excision repair. To this end, using DNA glycosylases from different structural families as an example—as well as apurinic/apyrimidinic endonuclease, which differs structurally and catalytically from DNA glycosylases—a comprehensive methodology is described in detail regarding studies on the mechanisms of action of DNA repair enzymes in humans and in Escherichia coli. This methodology is based on kinetic, thermodynamic, and mutational analyses of alterations in the conformation of molecules of an enzyme and of DNA during their interaction in real time. The described techniques can be used to analyze any protein–protein or protein–nucleic acid interactions.

AB - This review deals with modern approaches to systematic research on molecular-kinetic mechanisms of damage recognition and removal by pro- and eukaryotic enzymes of DNA base excision repair. To this end, using DNA glycosylases from different structural families as an example—as well as apurinic/apyrimidinic endonuclease, which differs structurally and catalytically from DNA glycosylases—a comprehensive methodology is described in detail regarding studies on the mechanisms of action of DNA repair enzymes in humans and in Escherichia coli. This methodology is based on kinetic, thermodynamic, and mutational analyses of alterations in the conformation of molecules of an enzyme and of DNA during their interaction in real time. The described techniques can be used to analyze any protein–protein or protein–nucleic acid interactions.

KW - AP endonuclease

KW - DNA damage

KW - DNA glycosylase

KW - base excision repair

KW - catalysis

KW - enzymatic activity

KW - fluorescence

KW - mechanism

KW - mutational analysis

KW - pre-steady-state kinetics

KW - thermodynamics

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85172252838&origin=inward&txGid=ee69744c8e417428e658e6261a3fba0f

UR - https://www.mendeley.com/catalogue/25c4bddb-9410-3adc-8ebf-77090df54ac5/

U2 - 10.3390/photonics10091033

DO - 10.3390/photonics10091033

M3 - Article

VL - 10

JO - Photonics

JF - Photonics

SN - 2304-6732

IS - 9

M1 - 1033

ER -

ID: 59279877