Methods for the analysis of protein-chromatin interactions
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Updated: Oct 2, 2026

Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes
Published on: October 2, 2017
Sarah J Brickwood1, Fiona A Myers, Simon P Chandler
1Sangamo Biosciences Inc., Point Richmond Tech Center, Richmond, CA 04804, USA.
Abstract:
The analysis of protein interactions with chromatin is vital for the understanding of DNA sequence recognition in vivo. Chromatin binding requires the interaction of proteins with DNA lying on the macromolecular protein surface of nucleosomes, a situation that can alter factor binding characteristics substantially when compared with naked DNA. It is therefore important to study these protein-DNA interactions in the context of a chromatin substrate, the more physiologically relevant binding situation. In this article we review techniques used in the investigation of protein interactions with defined nucleosomal templates.
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