Probing conformational change of T7 RNA polymerase and DNA complex by solid-state nanopores

doi:10.1088/1674-1056/27/11/118705

中国物理B ›› 2018, Vol. 27 ›› Issue (11): 118705-118705.doi: 10.1088/1674-1056/27/11/118705

• INTERDISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY • 上一篇下一篇

Probing conformational change of T7 RNA polymerase and DNA complex by solid-state nanopores

Xin Tong(童鑫), Rui Hu(胡蕊), Xiaoqing Li(李晓晴), Qing Zhao(赵清)

1 State Key Laboratory for Mesoscopic Physics and Electron Microscopy Laboratory, School of Physics, Peking University, Beijing 100871, China;
2 Collaborative Innovation Center of Quantum Matter, Beijing 100084, China

收稿日期:2018-06-19 修回日期:2018-08-14 出版日期:2018-11-05 发布日期:2018-11-05
通讯作者: Qing Zhao E-mail:zhaoqing@pku.edu.cn
基金资助:
Project supported by the National Natural Science Foundation of China (Grant Nos. 51622201, 91733301, and 61571015).

Probing conformational change of T7 RNA polymerase and DNA complex by solid-state nanopores

Xin Tong(童鑫)¹, Rui Hu(胡蕊)¹, Xiaoqing Li(李晓晴)¹, Qing Zhao(赵清)^1,2

1 State Key Laboratory for Mesoscopic Physics and Electron Microscopy Laboratory, School of Physics, Peking University, Beijing 100871, China;
2 Collaborative Innovation Center of Quantum Matter, Beijing 100084, China

Received:2018-06-19 Revised:2018-08-14 Online:2018-11-05 Published:2018-11-05
Contact: Qing Zhao E-mail:zhaoqing@pku.edu.cn
Supported by:
Project supported by the National Natural Science Foundation of China (Grant Nos. 51622201, 91733301, and 61571015).

摘要/Abstract

摘要：

Proteins are crucial to most biological processes, such as enzymes, and in various catalytic processes a dynamic motion is required. The dynamics of protein are embodied as a conformational change, which is closely related to the flexibility of protein. Recently, nanopore sensors have become accepted as a low cost and high throughput method to study the features of proteins. In this article, we used a SiN nanopore device to study the flexibility of T7 RNA polymerase (RNAP) and its complex with DNA promoter. By calculating full-width at half-maximum (FWHM) of Gaussian fits to the blockade histograms, we found that T7 RNAP becomes more flexible after binding DNA promoter. Moreover, the distribution of fractional current blockade suggests that flexibility alters due to a breath-like change of the volume.

关键词: solid-state nanopore, T7 RNA polymerase, conformational change, protein flexibility

Abstract:

Key words: solid-state nanopore, T7 RNA polymerase, conformational change, protein flexibility

中图分类号: (Single-molecule techniques)

87.80.Nj

62.23.St (Complex nanostructures, including patterned or assembled structures) 87.15.-v (Biomolecules: structure and physical properties)

童鑫, 胡蕊, 李晓晴, 赵清. Probing conformational change of T7 RNA polymerase and DNA complex by solid-state nanopores[J]. 中国物理B, 2018, 27(11): 118705-118705.

Xin Tong(童鑫), Rui Hu(胡蕊), Xiaoqing Li(李晓晴), Qing Zhao(赵清). Probing conformational change of T7 RNA polymerase and DNA complex by solid-state nanopores[J]. Chin. Phys. B, 2018, 27(11): 118705-118705.

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Probing conformational change of T7 RNA polymerase and DNA complex by solid-state nanopores

Probing conformational change of T7 RNA polymerase and DNA complex by solid-state nanopores

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