Domain-specific folding kinetics of staphylococcal nuclease observed through single-molecule FRET in a microfluidic mixer.
Domain-specific folding kinetics of staphylococcal nuclease observed through single-molecule FRET in a microfluidic mixer.
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DOI：
10.1002/cphc.201100652
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发表时间：
2011-12
期刊：
影响因子：
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通讯作者：
Zeyong Zhi;Pengcheng Liu;Peng Wang;Yanyi Huang;Xin Sheng Zhao
中科院分区：
文献类型：
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作者：
Zeyong Zhi;Pengcheng Liu;Peng Wang;Yanyi Huang;Xin Sheng Zhao
在这里，我们报道了我们在微流控混合器中的非平衡smFRET研究，以直接探测坍塌后从未折叠状态到自然折叠状态的转变速率。我们在选定的位置标记了供体和受体染料，以检测折叠景观中亚域和全局分子的构象重组的动力学。通过对展开和折叠状态的考察，动力学测量表明，不同的结构域采取不同的搜索路径来达到天然构象。
Herein, we report our non-equilibrium smFRET studies in a microfluidic mixer to directly probe the transition rate from the unfolded state to the native folded state after the collapse. We labeled donor and acceptor dyes at selected sites to detect the kinetics of the conformational reorganization of the subdomains and the global molecule in the refolding landscape. By examining the unfolded and folded states, the kinetic measurements suggested that different domains adopt different searching pathways to reach the native conformation.