title: Microscale thermophoresis for the assessment of nuclear protein-binding affinities.
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.
authors.affiliation: Department of Biochemistry, University of Cambridge, Cambridge, UK.
authors.forename: Wei
authors.initials: W
authors.lastname: Zhang
authors.forename: Stefan
authors.initials: S
authors.lastname: Duhr
authors.forename: Philipp
authors.initials: P
authors.lastname: Baaske
authors.forename: Ernest
authors.initials: E
authors.lastname: Laue
mesh_terms: D001671:Biochemistry / Q000379:methods*; D002021:Buffers; D005456:Fluorescent Dyes / Q000378:metabolism; D006801:Humans; D009687:Nuclear Proteins / Q000378:metabolism*; D011485:Protein Binding; D013194:Staining and Labeling; D013696:Temperature
chemical_list: D002021:Buffers; D005456:Fluorescent Dyes; D009687:Nuclear Proteins