@inbook{bc059f2203f94b46b38bb82426321722,
title = "Biochemical and biophysical methods for analysis of poly(ADP-ribose) polymerase 1 and its interactions with chromatin",
abstract = "Poly (ADP-Ribose) Polymerase I (PARP-1) is a first responder to DNA damage and participates in the regulation of gene expression. The interaction of PARP-1 with chromatin and DNA is complex and involves at least two different modes of interaction. In its enzymatically inactive state, PARP-1 binds native chromatin with similar affinity as it binds free DNA ends. Automodification of PARP-1 affects interaction with chromatin and DNA to different extents. Here we describe a series of biochemical and biophysical techniques to quantify and dissect the different binding modes of PARP-1 with its various substrates. The techniques listed here allow for high throughput and quantitative measurements of the interaction of different PARP-1 constructs (inactive and automodified) with chromatin and DNA damage models.",
keywords = "Analytical ultracentrifugation, Atomic force microscopy, Electrophoretic mobility shift assays, HI-FI FRET, Job plot, Multi-angle light scattering, PARP-1, Small angle X-ray scattering",
author = "Chass{\'e}, {Maggie H.} and Muthurajan, {Uma M.} and Clark, {Nicholas J.} and Kramer, {Michael A.} and Srinivas Chakravarthy and Thomas Irving and Karolin Luger",
note = "Publisher Copyright: {\textcopyright} 2017, Springer Science+Business Media LLC.",
year = "2017",
doi = "10.1007/978-1-4939-6993-7_16",
language = "English",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "231--253",
booktitle = "Methods in Molecular Biology",
}