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Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering

The molecular understanding of protein stabilization by the disaccharide trehalose in extreme temperature or hydration conditions is still debated. In the present study, we investigated the role of trehalose on the dynamics of the protein C-phycocyanin (C-PC) by neutron scattering. To single out the...

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Autores principales: Köper, Ingo, Combet, Sophie, Petry, Winfried, Bellissent-Funel, Marie-Claire
Formato: Texto
Lenguaje:English
Publicado: Springer-Verlag 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755759/
https://www.ncbi.nlm.nih.gov/pubmed/18185929
http://dx.doi.org/10.1007/s00249-007-0248-x
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author Köper, Ingo
Combet, Sophie
Petry, Winfried
Bellissent-Funel, Marie-Claire
author_facet Köper, Ingo
Combet, Sophie
Petry, Winfried
Bellissent-Funel, Marie-Claire
author_sort Köper, Ingo
collection PubMed
description The molecular understanding of protein stabilization by the disaccharide trehalose in extreme temperature or hydration conditions is still debated. In the present study, we investigated the role of trehalose on the dynamics of the protein C-phycocyanin (C-PC) by neutron scattering. To single out the motions of C-PC hydrogen (H) atoms in various trehalose/water environments, measurements were performed in deuterated trehalose and heavy water (D(2)O). We report that trehalose decreases the internal C-PC dynamics, as shown by a reduced diffusion coefficient of protein H atoms. By fitting the Elastic Incoherent Structure Factor—which gives access to the “geometry” of the internal proton motions—with the model of diffusion inside a sphere, we found that the presence of trehalose induces a significantly higher proportion of immobile C-PC hydrogens. We investigated, by elastic neutron scattering, the mean square displacements (MSDs) of deuterated trehalose/D(2)O-embedded C-PC as a function of temperature in the range of 40–318 K. Between 40 and ∼225 K, harmonic MSDs of C-PC are slightly smaller in samples containing trehalose. Above a transition temperature of ∼225 K, we observed anharmonic motions in all trehalose/water-coated C-PC samples. In the hydrated samples, MSDs are not significantly changed by addition of 15% trehalose but are slightly reduced by 30% trehalose. In opposition, no dynamical transition was detected in dry trehalose-embedded C-PC, whose hydrogen motions remain harmonic up to 318 K. These results suggest that a role of trehalose would be to stabilize proteins by inhibiting some fluctuations at the origin of protein unfolding and denaturation.
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spelling pubmed-27557592009-10-07 Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering Köper, Ingo Combet, Sophie Petry, Winfried Bellissent-Funel, Marie-Claire Eur Biophys J Original Paper The molecular understanding of protein stabilization by the disaccharide trehalose in extreme temperature or hydration conditions is still debated. In the present study, we investigated the role of trehalose on the dynamics of the protein C-phycocyanin (C-PC) by neutron scattering. To single out the motions of C-PC hydrogen (H) atoms in various trehalose/water environments, measurements were performed in deuterated trehalose and heavy water (D(2)O). We report that trehalose decreases the internal C-PC dynamics, as shown by a reduced diffusion coefficient of protein H atoms. By fitting the Elastic Incoherent Structure Factor—which gives access to the “geometry” of the internal proton motions—with the model of diffusion inside a sphere, we found that the presence of trehalose induces a significantly higher proportion of immobile C-PC hydrogens. We investigated, by elastic neutron scattering, the mean square displacements (MSDs) of deuterated trehalose/D(2)O-embedded C-PC as a function of temperature in the range of 40–318 K. Between 40 and ∼225 K, harmonic MSDs of C-PC are slightly smaller in samples containing trehalose. Above a transition temperature of ∼225 K, we observed anharmonic motions in all trehalose/water-coated C-PC samples. In the hydrated samples, MSDs are not significantly changed by addition of 15% trehalose but are slightly reduced by 30% trehalose. In opposition, no dynamical transition was detected in dry trehalose-embedded C-PC, whose hydrogen motions remain harmonic up to 318 K. These results suggest that a role of trehalose would be to stabilize proteins by inhibiting some fluctuations at the origin of protein unfolding and denaturation. Springer-Verlag 2008-01-08 2008-07 /pmc/articles/PMC2755759/ /pubmed/18185929 http://dx.doi.org/10.1007/s00249-007-0248-x Text en © EBSA 2007
spellingShingle Original Paper
Köper, Ingo
Combet, Sophie
Petry, Winfried
Bellissent-Funel, Marie-Claire
Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering
title Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering
title_full Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering
title_fullStr Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering
title_full_unstemmed Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering
title_short Dynamics of C-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering
title_sort dynamics of c-phycocyanin in various deuterated trehalose/water environments measured by quasielastic and elastic neutron scattering
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2755759/
https://www.ncbi.nlm.nih.gov/pubmed/18185929
http://dx.doi.org/10.1007/s00249-007-0248-x
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