Abstract
The rapid advance in our knowledge of cellular regulatory mechanisms, including those involving chromatin-based processes, stems in part from the development of biophysical techniques such as fluorescence spectroscopy, surface plasmon resonance (SPR), and isothermal titration calorimetry (ITC). Despite their widespread utility, each of these techniques has its pros and cons, and new techniques are still required. Here we describe the application of microscale thermophoresis (MST), a novel technique based on thermophoresis, to characterize the binding between histone peptides and a histone chaperone protein, in free solution, with high sensitivity and low sample consumption.
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Acknowledgements
This work was supported by the Wellcome Trust—grant 082010/Z/07/Z. We thank the PNAC facility in the Department of Biochemistry, University of Cambridge, for mass spectrometry and amino acid analysis.
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Zhang, W., Duhr, S., Baaske, P., Laue, E. (2014). Microscale Thermophoresis for the Assessment of Nuclear Protein-Binding Affinities. In: Stockert, J., Espada, J., Blázquez-Castro, A. (eds) Functional Analysis of DNA and Chromatin. Methods in Molecular Biology, vol 1094. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-706-8_21
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DOI: https://doi.org/10.1007/978-1-62703-706-8_21
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