Zhang Wei, Duhr Stefan, Baaske Philipp, Laue Ernest
Department of Biochemistry, University of Cambridge, Cambridge, UK.
Methods Mol Biol. 2014;1094:269-76. doi: 10.1007/978-1-62703-706-8_21.
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.
我们对细胞调控机制（包括那些涉及基于染色质的过程）的认识迅速进步，部分源于生物物理技术的发展，如荧光光谱法、表面等离子体共振（SPR）和等温滴定量热法（ITC）。尽管这些技术具有广泛的实用性，但每种技术都有其优缺点，仍然需要新技术。在这里，我们描述了微量热泳技术（MST）的应用，这是一种基于热泳的新技术，用于在游离溶液中以高灵敏度和低样品消耗来表征组蛋白肽与组蛋白伴侣蛋白之间的结合。
