Microfluidic Platform for Time-Resolved Characterization of Protein Higher-Order Structures and Dynamics Using Top-Down Mass Spectrometry-Reference-Cited by-同舟云学术

Microfluidic Platform for Time-Resolved Characterization of Protein Higher-Order Structures and Dynamics Using Top-Down Mass Spectrometry

Published:2022-05-18 Issue:21 Volume:94 Page:7520-7527
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Li Wen¹,Chaihu Lingxiao²³,Jiang Jialu²,Wu Bizhu¹,Zheng Xuan¹,Dai Rongrong²,Tian Ye³,Huang Yanyi³⁴^ORCID,Wang Guanbo³⁴^ORCID,Men Yongfan¹

Affiliation:

1. Research Center for Biomedical Optics and Molecular Imaging, Institute of Biomedical and Health Engineering, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China

2. School of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210023, China

3. Institute of Cell Analysis, Shenzhen Bay Laboratory, Shenzhen 518132, China

4. Biomedical Pioneering Innovation Centre, Peking University, Beijing 100871, China

Funder

Guangdong Science and Technology Department

Science, Technology and Innovation Commission of Shenzhen Municipality

National Natural Science Foundation of China

Guangdong Program

Shenzhen Bay Laboratory, Guangdong Province

Guangdong Provincial Key Laboratory of Biomedical Optical Imaging

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.2c00077

Reference80 articles.

1. Mass spectrometry-based methods to study protein architecture and dynamics

2. The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes

3. Bridging protein structure, dynamics, and function using hydrogen/deuterium‐exchange mass spectrometry

4. HDX-MS: An Analytical Tool to Capture Protein Motion in Action

5. Top-down hydrogen/deuterium exchange and ECD-stitched FTICR-MS for probing structural dynamics of a 29-kDa enzyme

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