Single-molecule study on conformational dynamics of M.HhaI-Reference-Cited by-同舟云学术

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Single-molecule study on conformational dynamics of M.HhaI

Published:2019 Issue:26 Volume:9 Page:14745-14749
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

He Shanshan¹²³⁴⁵,Yang Chen¹²³⁴⁵,Peng Sijia⁶⁷⁸⁹¹⁰,Chen Chunlai⁶⁷⁸⁹¹⁰^ORCID,Zhao Xin Sheng¹²³⁴⁵^ORCID

Affiliation:

1. Beijing National Laboratory for Molecular Sciences

2. State Key Laboratory for Structural Chemistry of Unstable and Stable Species

3. Department of Chemical Biology

4. College of Chemistry and Molecular Engineering

5. Peking University

6. School of Life Sciences

7. Tsinghua-Peking Joint Center for Life Sciences

8. Beijing Advanced Innovation Center for Structural Biology

9. Tsinghua University

10. Beijing 100084

Abstract

Huge conformational rearrangements in M.HhaI were observed by a single-molecule study.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/RA/C9RA00021F

Reference17 articles.

1. Dynamic DNA methylation: In the right place at the right time

2. Hhal methyltransferase flips its target base out of the DNA helix

3. Protein-facilitated base flipping in DNA by cytosine-5-methyltransferase

4. Observing an Induced-fit Mechanism during Sequence-specific DNA Methylation

5. Determinants of Precatalytic Conformational Transitions in the DNA Cytosine Methyltransferase M.HhaI

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1. Base Dynamics in the HhaI Protein Binding Site;The Journal of Physical Chemistry B;2023-08-10

2. DeepFRET, a software for rapid and automated single-molecule FRET data classification using deep learning;eLife;2020-11-03

3. Molecular mechanism of networking among DegP, Skp and SurA in periplasm for biogenesis of outer membrane proteins;Biochemical Journal;2020-08-19

4. DeepFRET: Rapid and automated single molecule FRET data classification using deep learning;2020-06-27

5. Molecular mechanism of SurA’s chaperoning function to outer membrane proteins revealed by purification-after-crosslinking single-molecule FRET;Science China Chemistry;2020-05-20

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