Mean-Square Displacement Relationship in Bioprotectant Systems by Elastic Neutron Scattering

Magazù, Salvatore; Maisano, G.; Migliardo, F.; Mondelli, C.

doi:10.1016/s0006-3495(04)74372-6

Cited by 89 publications

(116 citation statements)

References 44 publications

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“…The interpretative model to describe the observed behavior can be visualized as follows for the elementary flow process (the α-relaxation): an atom jumps in the fast processes (β-relaxation motions) with a Gaussian probability distribution characterized by a mean-square amplitude <u 2 > loc , defined as the difference between the mean square displacement of the ordered and disordered phase [15]:…”

Section: Resultsmentioning

confidence: 99%

“…It has been demonstrated that a linear relationship between M M and m exists [15]. On the basis of the relationships introduced, we will try now to get information on the fragility degree of the glassy systems which when host proteins are present show an Intensity (a.…”

Section: Resultsmentioning

confidence: 99%

“…Previous analyses of the mean square displacement obtained on the three bioprotectant homologous disaccharides suggest that trehalose is characterized in respect to maltose and sucrose by a lower fragility, namely by a higher structural resistance to temperature changes in approaching the glass transition temperature [15]. These findings indicate a correlation between fragility degree and bioprotection effectiveness and could give also an explanation for the better preservation provided by several bioprotectants.…”

Section: Introductionmentioning

confidence: 80%

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Study of solvent–protein coupling effects by neutron scattering

et al. 2009

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The present work aims to characterize the dynamical behavior of proteins immersed in bio-preserving liquids and glasses. For this purpose, the protein dUTPase was chosen, while the selected solvents were glycerol, a triol, and some homologous disaccharides, i.e., trehalose, maltose, and sucrose, which are known to be very effective bio-preserving agents. The results highlight that the disaccharides show a slowing down effect on the water dynamics, which is stronger for trehalose than in the case of the other disaccharides. Furthermore, a characterization of the medium which hosts the protein is performed by using an operative definition of fragility based on the mean square displacement extracted by elastic incoherent neutron scattering, which is directly connected to Angell's kinetic fragility based on the viscosity. Finally, a study of the dynamics of the protein sequestered within the solvents is performed. The result shows that the protein dynamics is coupled with that of the surrounding matrix.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 80%

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Study of solvent–protein coupling effects by neutron scattering

et al. 2009

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“…(5) allows also a very intuitive understanding of the effect of different instrumental time resolution on the usually explored apparent MSD measured at ω = 0 (see also Ref. [4,14]):…”

Section: Dependence Of Umentioning

confidence: 99%

“…Well-known examples include the dynamics in glass-forming systems [1][2][3] and bioprotectant disaccharides [4] as well as the protein dynamical transition [5,6], in particular the coupling of protein dynamics to the environment [7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

A generalized mean-squared displacement from inelastic fixed window scans of incoherent neutron scattering as a model-free indicator of anomalous diffusion confinement

Roosen-Runge

Seydel

2015

EPJ Web of Conferences

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Abstract. Elastic fixed window scans of incoherent neutron scattering are an established and frequently employed method to study dynamical changes, usually over a broad temperature range or during a process such as a conformational change in the sample. In particular, the apparent mean-squared displacement can be extracted via a model-free analysis based on a solid physical interpretation as an effective amplitude of molecular motions. Here, we provide a new account of elastic and inelastic fixed window scans, defining a generalized mean-squared displacement for all fixed energy transfers. We show that this generalized mean-squared displacement in principle contains all information on the real mean-square displacement accessible in the instrumental time window. The derived formula provides a clear understanding of the effects of instrumental resolution on the apparent mean-squared displacement. Finally, we show that the generalized mean-square displacement can be used as a model-free indicator on confinement effects within the instrumental time window.

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How Ligand Binding Affects the Dynamical Transition Temperature in Proteins

2020

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The biochemical functions of proteins are activated at the protein glass transition temperature, which has been proposed to be dependent upon protein-water interactions. However, at the molecular level it is unclear how ligand binding to welldefined binding sites can influence this transition temperature. We thus report molecular dynamics (MD) simulations of the ɛ subunit from thermophilic Bacillus PS3 in the ATP-free and ligand-bound states over a range of temperatures from 20 to 300 K, to study the influence of ligand association upon the transition temperature. We also measure the protein mean square displacement (MSD) in each state, which is well established as a means to quantify this dynamical temperature dependence. We find that the transition temperature is largely unaffected by ligand association, but the MSD beyond the transition temperature increases more rapidly in the ATP-free state. Our data suggests that ligands can effectively "shield" a binding site from solvent, and hence stabilize protein domains with increasing temperature.

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Mean-Square Displacement Relationship in Bioprotectant Systems by Elastic Neutron Scattering

Cited by 89 publications

References 44 publications

Study of solvent–protein coupling effects by neutron scattering

Study of solvent–protein coupling effects by neutron scattering

A generalized mean-squared displacement from inelastic fixed window scans of incoherent neutron scattering as a model-free indicator of anomalous diffusion confinement

How Ligand Binding Affects the Dynamical Transition Temperature in Proteins

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