Cargando…

Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra

Hydration effects on protein dynamics were investigated by comparing the frequency dependence of the calculated neutron scattering spectra between full and minimal hydration states at temperatures between 100 and 300 K. The protein boson peak is observed in the frequency range 1–4 meV at 100 K in bo...

Descripción completa

Detalles Bibliográficos
Autores principales: Joti, Yasumasa, Nakagawa, Hiroshi, Kataoka, Mikio, Kitao, Akio
Formato: Texto
Lenguaje:English
Publicado: The Biophysical Society 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2480692/
https://www.ncbi.nlm.nih.gov/pubmed/18310244
http://dx.doi.org/10.1529/biophysj.107.118042
_version_ 1782157961450225664
author Joti, Yasumasa
Nakagawa, Hiroshi
Kataoka, Mikio
Kitao, Akio
author_facet Joti, Yasumasa
Nakagawa, Hiroshi
Kataoka, Mikio
Kitao, Akio
author_sort Joti, Yasumasa
collection PubMed
description Hydration effects on protein dynamics were investigated by comparing the frequency dependence of the calculated neutron scattering spectra between full and minimal hydration states at temperatures between 100 and 300 K. The protein boson peak is observed in the frequency range 1–4 meV at 100 K in both states. The peak frequency in the minimal hydration state shifts to lower than that in the full hydration state. Protein motions with a frequency higher than 4 meV were shown to undergo almost harmonic motion in both states at all temperatures simulated, whereas those with a frequency lower than 1 meV dominate the total fluctuations above 220 K and contribute to the origin of the glass-like transition. At 300 K, the boson peak becomes buried in the quasielastic contributions in the full hydration state but is still observed in the minimal hydration state. The boson peak is observed when protein dynamics are trapped within a local minimum of its energy surface. Protein motions, which contribute to the boson peak, are distributed throughout the whole protein. The fine structure of the dynamics structure factor is expected to be detected by the experiment if a high resolution instrument (<∼20 μeV) is developed in the near future.
format Text
id pubmed-2480692
institution National Center for Biotechnology Information
language English
publishDate 2008
publisher The Biophysical Society
record_format MEDLINE/PubMed
spelling pubmed-24806922008-07-23 Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra Joti, Yasumasa Nakagawa, Hiroshi Kataoka, Mikio Kitao, Akio Biophys J Proteins Hydration effects on protein dynamics were investigated by comparing the frequency dependence of the calculated neutron scattering spectra between full and minimal hydration states at temperatures between 100 and 300 K. The protein boson peak is observed in the frequency range 1–4 meV at 100 K in both states. The peak frequency in the minimal hydration state shifts to lower than that in the full hydration state. Protein motions with a frequency higher than 4 meV were shown to undergo almost harmonic motion in both states at all temperatures simulated, whereas those with a frequency lower than 1 meV dominate the total fluctuations above 220 K and contribute to the origin of the glass-like transition. At 300 K, the boson peak becomes buried in the quasielastic contributions in the full hydration state but is still observed in the minimal hydration state. The boson peak is observed when protein dynamics are trapped within a local minimum of its energy surface. Protein motions, which contribute to the boson peak, are distributed throughout the whole protein. The fine structure of the dynamics structure factor is expected to be detected by the experiment if a high resolution instrument (<∼20 μeV) is developed in the near future. The Biophysical Society 2008-06-01 2008-02-29 /pmc/articles/PMC2480692/ /pubmed/18310244 http://dx.doi.org/10.1529/biophysj.107.118042 Text en Copyright © 2008, Biophysical Society This is an Open Access article distributed under the terms of the Creative Commons-Attribution Noncommercial License (http://creativecommons.org/licenses/by-nc/2.0/), which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Proteins
Joti, Yasumasa
Nakagawa, Hiroshi
Kataoka, Mikio
Kitao, Akio
Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra
title Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra
title_full Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra
title_fullStr Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra
title_full_unstemmed Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra
title_short Hydration Effect on Low-Frequency Protein Dynamics Observed in Simulated Neutron Scattering Spectra
title_sort hydration effect on low-frequency protein dynamics observed in simulated neutron scattering spectra
topic Proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2480692/
https://www.ncbi.nlm.nih.gov/pubmed/18310244
http://dx.doi.org/10.1529/biophysj.107.118042
work_keys_str_mv AT jotiyasumasa hydrationeffectonlowfrequencyproteindynamicsobservedinsimulatedneutronscatteringspectra
AT nakagawahiroshi hydrationeffectonlowfrequencyproteindynamicsobservedinsimulatedneutronscatteringspectra
AT kataokamikio hydrationeffectonlowfrequencyproteindynamicsobservedinsimulatedneutronscatteringspectra
AT kitaoakio hydrationeffectonlowfrequencyproteindynamicsobservedinsimulatedneutronscatteringspectra