One-step asparaginyl endopeptidase (<i>Oa</i>AEP1)-based protein immobilization for single-molecule force spectroscopy-Reference-Cited by-同舟云学术

One-step asparaginyl endopeptidase (OaAEP1)-based protein immobilization for single-molecule force spectroscopy

Published:2022 Issue:10 Volume:3 Page:1276-1281
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Ding Xuan¹²^ORCID,Wang Ziyi³,Zheng Bin³,Shi Shengchao³,Deng Yibing³,Yu Hanyang¹^ORCID,Zheng Peng³^ORCID

Affiliation:

1. Department of Biomedical Engineering, College of Engineering and Applied Sciences, Nanjing University, 163 Xianlin Road, Nanjing, Jiangsu 210023, P. R. China

2. State Key Laboratory of Analytical Chemistry for Life Science, Nanjing University, Nanjing, Jiangsu 210023, P. R. China

3. State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu 210023, P. R. China

Abstract

Enzymatic protein ligation has become the most powerful and widely used method for high-precision atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) study of protein mechanics.

Funder

Natural Science Foundation of Jiangsu Province

National Natural Science Foundation of China

Fundamental Research Funds for the Central Universities

Publisher

Royal Society of Chemistry (RSC)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CB/D2CB00135G

Reference65 articles.

1. Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance