Rapidly determining the 3D structure of proteins by surface-enhanced Raman spectroscopy

Author:

Ma Hao12ORCID,Yan Sen12ORCID,Lu Xinyu12,Bao Yi-Fan12,Liu Jia1,Liao Langxing1,Dai Kun3ORCID,Cao Maofeng12,Zhao Xiaojiao12,Yan Hao1ORCID,Wang Hai-Long2,Peng Xiaohui12,Chen Ningyu12,Feng Huishu12,Zhu Lilin12,Yao Guangbao3ORCID,Fan Chunhai3ORCID,Wu De-Yin1ORCID,Wang Binju1ORCID,Wang Xiang12ORCID,Ren Bin12ORCID

Affiliation:

1. State Key Laboratory of Physical Chemistry of Solid Surfaces, Collaborative Innovation Center of Chemistry for Energy Materials (i-ChEM), Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China.

2. Innovation Laboratory for Sciences and Technologies of Energy Materials of Fujian Province (IKKEM), Xiamen 361005, China.

3. School of Chemistry and Chemical Engineering, Frontiers Science Center for Transformative Molecules, National Center for Translational Medicine, Shanghai Jiao Tong University, Shanghai 200240, China.

Abstract

Despite great advances in protein structure analysis, label-free and ultrasensitive methods to obtain the natural and dynamic three-dimensional (3D) structures are still urgently needed. Surface-enhanced Raman spectroscopy (SERS) can be a good candidate, whereas the complexity originated from the interactions between the protein and the gradient surface electric field makes it extremely challenging to determine the protein structure. Here, we propose a deciphering strategy for accurate determination of 3D protein structure from experimental SERS spectra in seconds by simply summing SERS spectra of isolated amino acids in electric fields of different strength with their orientations in protein. The 3D protein structure can be reconstructed by comparing the experimental spectra obtained in a well-defined gap-mode SERS configuration with the simulated spectra. The gradient electric field endows SERS with a unique advantage to section biomolecules with atomic precision, which makes SERS a competent tool for monitoring biomolecular events under physiological conditions.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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