0537940 - MBÚ 2021 RIV US eng M - Monography Chapter
Filandrová, Růžena - Kavan, Daniel - Kádek, Alan - Novák, Petr - Man, Petr
Studying Protein-DNA Interactions by Hydrogen/Deuterium Exchange Mass Spectrometry.
Multiprotein Complexes. Vol. 2247. New York: Springer, 2021 - (Poterszman, A.), s. 193-219. Methods in Molecular Biology. ISBN 978-1-0716-1125-8
R&D Projects: GA ČR(CZ) GA16-24309S; GA ČR(CZ) GA16-20860S; GA MŠMT(CZ) LQ1604; GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) LQ1604
Institutional support: RVO:61388971
Keywords : DNA * Hydrogen/deuterium exchange * Protein–DNA binding * Structural mass spectrometry * Transcription factor
OECD category: Biochemistry and molecular biology
Result website:
https://link.springer.com/protocol/10.1007/978-1-0716-1126-5_11DOI: https://doi.org/10.1007/978-1-0716-1126-5_11

Protein hydrogen/deuterium exchange (HDX) coupled to mass spectrometry (MS) can be used to study interactions of proteins with various ligands, to describe the effects of mutations, or to reveal structural responses of proteins to different experimental conditions. It is often described as a method with virtually no limitations in terms of protein size or sample composition. While this is generally true, there are, however, ligands or buffer components that can significantly complicate the analysis. One such compound, that can make HDX-MS troublesome, is DNA. In this chapter, we will focus on the analysis of protein–DNA interactions, describe the detailed protocol, and point out ways to overcome the complications arising from the presence of DNA.
Permanent Link: http://hdl.handle.net/11104/0315768