Modeling 15N NMR chemical shift changes in protein backbone with pressure-Reference-Cited by-同舟云学术

Modeling 15N NMR chemical shift changes in protein backbone with pressure

Published:2016-08-28 Issue:8 Volume:145 Page:085104
ISSN:0021-9606
Container-title:The Journal of Chemical Physics
language:en
Short-container-title:J. Chem. Phys.

Author:

La Penna Giovanni¹^ORCID,Mori Yoshiharu²,Kitahara Ryo³,Akasaka Kazuyuki⁴,Okamoto Yuko⁵

Affiliation:

1. Institute for Chemistry of Organo–Metallic Compounds (ICCOM), National Research Council of Italy (Cnr), Via Madonna del Piano 10, I-50019 Sesto Fiorentino, Firenze, Italy

2. Theoretical and Computational Molecular Science, Institute for Molecular Science, 38 Nishigo-Naka, Myodaiji, Okazaki, 444-8585, Japan

3. College of Pharmaceutical Sciences, Ritsumeikan University, 1-1-1 Noji-higashi, Kusatsu 525-8577, Japan

4. Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, 1-5 Hangi-cho, Shimogamo, Sakyo-ku, Kyoto, Kyoto 606-8522, Japan

5. Department of Physics, School of Science, Nagoya University, Furo-cho, Chikusa-ku Nagoya, Aichi 464-8602, Japan

Funder

National research council of Italy

Ministry of Education, Culture, Sports, Science, and Technology (MEXT)

Publisher

AIP Publishing

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference57 articles.

1. J. Cavanagh, W. F. Fairbrother, A. G. PalmerIII, and N. J. Skelton, Protein NMR Spectroscopy (Academic Press, San Diego, USA , 1996).

2. Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network

3. Effect of Pressure on Individual Hydrogen Bonds in Proteins. Basic Pancreatic Trypsin Inhibitor

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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