Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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.
в: Photonics, Том 10, № 9, 1033, 09.2023.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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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