High temperature and pressure influence the interdomain orientation of Nip7 proteins from P. abyssi and P. furiosus: MD simulations-Reference-Cited by-同舟云学术

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High temperature and pressure influence the interdomain orientation of Nip7 proteins from P. abyssi and P. furiosus: MD simulations

Published:2017-01-04 Issue:1 Volume:36 Page:68-82
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Medvedev Kirill E.¹²^ORCID,Kolchanov Nikolay A.¹³,Afonnikov Dmitry A.¹³

Affiliation:

1. Systems Biology Department, Institute of Cytology and Genetics SB RAS, Prospekt Lavrentyeva 10, Novosibirsk 630090, Russia

2. Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA

3. Chair of Informational Biology, Novosibirsk State University, Pirogova str. 2, Novosibirsk 630090, Russia

Funder

Russian Science Foundation

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2016.1268070

Reference47 articles.

1. Accelrys Discovery Studio. (2009). Version 2.5. San Diego, CA: Accelrys.

2. Novel Predicted RNA-Binding Domains Associated with the Translation Machinery

3. Structural dynamics of full-length retroviral integrase: a molecular dynamics analysis

4. KCTD5 is endowed with large, functionally relevant, interdomain motions

5. Structural and Functional Aspects of Domain Motions in Proteins

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