2024-03-28T17:40:26Z
https://nagoya.repo.nii.ac.jp/oai
oai:nagoya.repo.nii.ac.jp:00026928
2023-01-16T04:17:35Z
336:695:696
Modeling 15N NMR chemical shift changes in protein backbone with pressure
La Penna, Giovanni
88229
Mori, Yoshiharu
88230
Kitahara, Ryo
88231
Akasaka, Kazuyuki
88232
Okamoto, Yuko
88233
Nitrogen chemical shift is a useful parameter for determining the backbone three-dimensional structure of proteins. Empirical models for fast calculation of N chemical shift are improving their reliability, but there are subtle effects that cannot be easily interpreted. Among these, the effects of slight changes in hydrogen bonds, both intramolecular and with water molecules in the solvent, are particularly difficult to predict. On the other hand, these hydrogen bonds are sensitive to changes in protein environment. In this work, the change of N chemical shift with pressure for backbone segments in the protein ubiquitin is correlated with the change in the population of hydrogen bonds involving the backbone amide group. The different extent of interaction of protein backbone with the water molecules in the solvent is put in evidence.
journal article
AIP Publishing
2016-08-28
application/pdf
The Journal of Chemical Physics
8
145
085104
0021-9606
https://nagoya.repo.nii.ac.jp/record/26928/files/1_4961507.pdf
eng
https://doi.org/10.1063/1.4961507
Copyright 2016 American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and AIP Publishing.The following article appeared in (The Journal of Chemical Physics. v.145, n.8, 2016, p.085104) and may be found at (http://dx.doi.org/10.1063/1.4961507).