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Title: Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diffraction and inelastic X-ray scattering

Abstract

We investigated hydrated antifreeze protein type III (AFP III) powder with a hydration level h (=mass of water/mass of protein) of 0.4 in the temperature range between 180 K and 298 K using X-ray diffraction and inelastic X-ray scattering (IXS). The X-ray diffraction data showed smooth, largely monotonic changes between 180 K and 298 K without freezing water. Meanwhile, the collective dynamics observed by IXS showed a strong change in the sound velocity at 180 K, after being largely temperature independent at higher temperatures (298–220 K). We interpret this change in terms of the dynamic transition previously discussed using other probes including THz IR absorption spectroscopy and incoherent elastic and quasi-elastic neutron scattering. This finding suggests that the dynamic transition of hydrated proteins is observable on the subpicosecond time scale as well as nano- and pico-second scales, both in collective dynamics from IXS and single particle dynamics from neutron scattering. Moreover, it is most likely that the dynamic transition of hydrated AFP III is not directly correlated with its hydration structure.

Authors:
 [1];  [2]; ;  [3];  [1]
  1. Department of Chemistry, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka 814-0180 (Japan)
  2. Materials Dynamics Laboratory, RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148 (Japan)
  3. Research and Utilization Division, Japan Synchrotron Radiation Research Institute, SPring-8, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198 (Japan)
Publication Date:
OSTI Identifier:
22657891
Resource Type:
Journal Article
Journal Name:
Journal of Chemical Physics
Additional Journal Information:
Journal Volume: 144; Journal Issue: 13; Other Information: (c) 2016 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0021-9606
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ABSORPTION SPECTROSCOPY; HYDRATION; INELASTIC SCATTERING; NEUTRON DIFFRACTION; PROTEINS; X-RAY DIFFRACTION

Citation Formats

Yoshida, Koji, Baron, Alfred Q. R., Uchiyama, Hiroshi, Tsutsui, Satoshi, Yamaguchi, Toshio, and Advanced Materials Institute, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka 814-0180. Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diffraction and inelastic X-ray scattering. United States: N. p., 2016. Web. doi:10.1063/1.4944987.
Yoshida, Koji, Baron, Alfred Q. R., Uchiyama, Hiroshi, Tsutsui, Satoshi, Yamaguchi, Toshio, & Advanced Materials Institute, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka 814-0180. Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diffraction and inelastic X-ray scattering. United States. https://doi.org/10.1063/1.4944987
Yoshida, Koji, Baron, Alfred Q. R., Uchiyama, Hiroshi, Tsutsui, Satoshi, Yamaguchi, Toshio, and Advanced Materials Institute, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka 814-0180. 2016. "Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diffraction and inelastic X-ray scattering". United States. https://doi.org/10.1063/1.4944987.
@article{osti_22657891,
title = {Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diffraction and inelastic X-ray scattering},
author = {Yoshida, Koji and Baron, Alfred Q. R. and Uchiyama, Hiroshi and Tsutsui, Satoshi and Yamaguchi, Toshio and Advanced Materials Institute, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku, Fukuoka 814-0180},
abstractNote = {We investigated hydrated antifreeze protein type III (AFP III) powder with a hydration level h (=mass of water/mass of protein) of 0.4 in the temperature range between 180 K and 298 K using X-ray diffraction and inelastic X-ray scattering (IXS). The X-ray diffraction data showed smooth, largely monotonic changes between 180 K and 298 K without freezing water. Meanwhile, the collective dynamics observed by IXS showed a strong change in the sound velocity at 180 K, after being largely temperature independent at higher temperatures (298–220 K). We interpret this change in terms of the dynamic transition previously discussed using other probes including THz IR absorption spectroscopy and incoherent elastic and quasi-elastic neutron scattering. This finding suggests that the dynamic transition of hydrated proteins is observable on the subpicosecond time scale as well as nano- and pico-second scales, both in collective dynamics from IXS and single particle dynamics from neutron scattering. Moreover, it is most likely that the dynamic transition of hydrated AFP III is not directly correlated with its hydration structure.},
doi = {10.1063/1.4944987},
url = {https://www.osti.gov/biblio/22657891}, journal = {Journal of Chemical Physics},
issn = {0021-9606},
number = 13,
volume = 144,
place = {United States},
year = {Thu Apr 07 00:00:00 EDT 2016},
month = {Thu Apr 07 00:00:00 EDT 2016}
}