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Nano Research 2016,9 (9) : 2551-2560 https://doi.org/10.1007/s12274-016-1141-7
Research Article | Issue | Published: 15 June 2016
Sub-molecular features of single proteins in solution resolved with scanning tunneling microscopy
Show Author's Information Jihao Wang1,2,§,  Lei Zhang1,§,  Chen Hu1,  Qingsong Liu1,  Yubin Hou1,  Xin Zhang1( ),  Qingyou Lu1,2,3( )
High Magnetic Field LaboratoryChinese Academy of Sciences and University of Science and Technology of ChinaHefei230026China
Hefei National Laboratory for Physical Sciences at the MicroscaleUniversity of Science and Technology of ChinaHefei230026China
Collaborative Innovation Center of Advanced MicrostructuresNanjing UniversityNanjing210093China

§These authors contributed equally to this work.

Keywords:
liquid-phase scanning tunneling microscopy (STM), STM imaging under physiological conditions, protein molecule, sub-molecular resolution
Cite this article:
J. Wang, L. Zhang, C. Hu, et al. Sub-molecular features of single proteins in solution resolved with scanning tunneling microscopy. Nano Research. 2016, 9 (9) : 2551-2560. https://doi.org/10.1007/s12274-016-1141-7.
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Abstract Full text Electronic supplementary material About this article

Scanning tunneling microscopy (STM) can be used to image individual biological molecules, such as proteins, in vacuum or air. This requires sample dehydration and thus may not reflect the native state of the molecule. Extensive efforts have been made to image single proteins in solution using STM; however, the images have revealed only round or oval shapes with no sub-molecular details. Here, we present the sub-molecular features of streptavidin proteins under physiological conditions using a homebuilt low-leakage-current and highstability liquid phase STM. The N-lobe, C-lobe, and C-terminal tail of the epidermal growth factor receptor kinase domains were also resolved in solution. Our results demonstrate that the structure, morphology, and dynamics of a protein molecule can be examined under physiological conditions by the STM.

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Publication history

Received: 15 February 2016
Revised: 06 May 2016
Accepted: 09 May 2016
Published: 15 June 2016
Issue date: September 2016

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© Tsinghua University Press and Springer‐Verlag Berlin Heidelberg 2016

Acknowledgements

Acknowledgements

This work was supported by the Chinese Academy of Sciences "Hundred Talent program" and National Natural Science Foundation of China (No. U1532151) to X. Z. and by Chinese national high magnetic field facilities, the Fundamental Research Funds for the Central Universities (No. WK2340000035) and National Natural Science Foundation of China (Nos. U1232210, 11204306, and 11374278) to Q. Y. L.

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