Conformational changes of ubiquitin under high pressure conditions: A pressure simulated tempering molecular dynamics study-Reference-Cited by-同舟云学术

Conformational changes of ubiquitin under high pressure conditions: A pressure simulated tempering molecular dynamics study

Published:2017-04-08 Issue:15 Volume:38 Page:1167-1173
ISSN:0192-8651
Container-title:Journal of Computational Chemistry
language:en
Short-container-title:J. Comput. Chem.

Author:

Mori Yoshiharu¹,Okamoto Yuko¹²³⁴⁵^ORCID

Affiliation:

1. Department of Physics, Graduate School of Science; Nagoya University; Nagoya Aichi 464-8602 Japan

2. JST-CREST; Nagoya Aichi 464-8602 Japan

3. Structural Biology Research Center, Graduate School of Science, Nagoya University; Nagoya Aichi 464-8602 Japan

4. Center for Computational Science, Graduate School of Engineering, Nagoya University; Nagoya Aichi 464-8603 Japan

5. Information Technology Center, Nagoya University; Nagoya Aichi 464-8601 Japan

Funder

Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan (JSPS Fellows, for Scientific Research on Innovative Areas [“Dynamical Ordering and Integrated Functions”])

Publisher

Wiley

Subject

Computational Mathematics,General Chemistry

Reference73 articles.

1. Pressure provides new insights into protein folding, dynamics and structure

2. Cavities determine the pressure unfolding of proteins

3. Two Folded Conformers of Ubiquitin Revealed by High-Pressure NMR

4. Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding

5. NMR Snapshots of a Fluctuating Protein Structure: Ubiquitin at 30 bar–3 kbar

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