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ANALYZING DNA-PROTEIN COMPLEXES’ STABILITY USING FLUORESCENCE POLARIZATION TO FACILITATE SAMPLE PREPARATION FOR ELECTRON MICROSCOPYтезисы доклада Тезисы
- Авторы: Фескин П.Г., Мамаева Н.Ю., Шайтан А.К.
- Сборник: RUSSIAN INTERNATIONAL CONFERENCE ON CRYO-ELECTRON MICROSCOPY 2023 JUNE 4-7 (RICCEM 2023) BOOK OF ABSTRACTS
- Тезисы
- Год издания: 2023
- Первая страница: 18
- Последняя страница: 18
- Аннотация: DNA-protein interactions play crucial role in functioning of living systems, including genomes of all living organisms. Electron microscopy is a popular technique that is often used to study structures of DNA-protein complexes. To efficiently prepare samples of these complexes for EM one requires some prior knowledge of the binding strength between DNA and protein. To date a lot of methods for detecting protein-DNA interactions have been developed. One approach relies on fluorescently labeled molecules: upon interaction of the labeled binders the changes in the fluorescence intensity or polarization may be detected. Fluorescencebased methods allow for a quantitative estimate of binding constants directly in the bulk solution. In this work we describe an experimental protocol based of fluorescence polarization measurements and present a data processing algorithm (developed by us using Python programming language), which allows to estimate binding constants from the experimental data and accounts properly for the background signal and measurement uncertainties.
- Добавил в систему: Фескин Павел Григорьевич