Department of Biochemistry G.Moruzzi, University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.
Bioinformatics. 2011 Feb 1;27(3):423-5. doi: 10.1093/bioinformatics/btq663. Epub 2010 Dec 1.
Single-molecule force spectroscopy has facilitated the experimental investigation of biomolecular force-coupled kinetics, from which the kinetics at zero force can be extrapolated via explicit theoretical models. The atomic force microscope (AFM) in particular is routinely used to study protein unfolding kinetics, but only rarely protein folding kinetics. The discrepancy arises because mechanical protein refolding studies are more technically challenging.
We developed software that can drive and analyse mechanical refolding experiments when used with the commercial AFM setup 'Picoforce AFM', Bruker (previously Digital Instruments). We expect the software to be easily adaptable to other AFM setups. We also developed an improved method for the statistical characterization of protein folding kinetics, and implemented it into an AFM-independent software module.
Software and documentation are available at http://code.google.com/p/refolding under Apache License 2.0.
单分子力谱学促进了生物分子力耦合动力学的实验研究，通过明确的理论模型可以推断零力下的动力学。原子力显微镜（AFM）特别常用于研究蛋白质解折叠动力学，但很少用于研究蛋白质折叠动力学。这种差异的出现是因为机械蛋白重折叠研究更具技术挑战性。
我们开发了一款软件，可以在与商业 AFM 设备 'Picoforce AFM'（原 Digital Instruments）结合使用时驱动和分析机械重折叠实验。我们预计该软件可以轻松适用于其他 AFM 设备。我们还开发了一种改进的蛋白质折叠动力学统计特征描述方法，并将其实现为一个与 AFM 无关的软件模块。
软件和文档可在 Apache License 2.0 下从 http://code.google.com/p/refolding 获得。
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