The folding mechanism and key metastable state identification of the PrP127–147 monomer studied by molecular dynamics simulations and Markov state model analysis-Reference-Cited by-同舟云学术

The folding mechanism and key metastable state identification of the PrP127–147 monomer studied by molecular dynamics simulations and Markov state model analysis

Published:2017 Issue:18 Volume:19 Page:11249-11259
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Zhou Shuangyan¹²³⁴,Wang Qianqian⁵⁶⁷⁸⁴,Wang Yuwei⁵⁶⁷⁸⁴,Yao Xiaojun⁵⁶⁷⁸⁴,Han Wei⁹¹⁰¹¹¹²⁴,Liu Huanxiang¹²³⁴^ORCID

Affiliation:

1. School of Pharmacy

2. Lanzhou University

3. Lanzhou 730000

4. China

5. State Key Laboratory of Quality Research in Chinese Medicine

6. Macau Institute for Applied Research in Medicine and Health

7. Macau University of Science and Technology

8. Taipa

9. Key Laboratory of Chemical Genomics

10. School of Chemical biology and Biotechnology

11. Beijing University Shenzhen Graduate School

12. Shenzhen

Abstract

MD simulation combined with MSM analysis was employed to investigate the structural dynamics and the folding mechanism of the key fragment 127–147 monomer of prion protein.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CP/C7CP01521F

Reference60 articles.

1. Human prion diseases and bovine spongiform encephalopathy (BSE)

2. Prion Diseases of Humans and Animals: Their Causes and Molecular Basis

3. Nobel Lecture: Prions

4. Iatrogenic Creutzfeldt-Jakob disease at the millennium

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