Neutron Inelastic Scattering as a High‐Resolution Vibrational Spectroscopy: New Tool for the Study of Protein Dynamics

Kataoka, Mikio; Kamikubo, Hironari; Parker, Stewart F.; Smith, Jeremy C.

doi:10.1155/2003/907042

Cited by 13 publications

(3 citation statements)

References 15 publications

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“…As described in ref , TOSCA has revealed itself to give detailed results combined to optical spectroscopic techniques such as Raman spectroscopy due to its design associating a single momentum transfer with each energy transfer. Furthermore TOSCA has been successfully used for investigating biological systems, such as globular proteins, − collagen and model polypeptides , and interfacial water. , …”

Section: Methodsmentioning

confidence: 99%

Vibrational Properties of Bioprotectant Mixtures of Trehalose and Glycerol

2011

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In this work vibrational spectra of mixtures of two glass-forming bioprotectant systems, i.e., trehalose and glycerol, are collected at very low temperature by using the indirect geometry time-of-flight (t.o.f.) TOSCA spectrometer at the ISIS Pulse Neutron Facility (Rutherford Appleton Laboratory, Oxford, U.K.). The main aim of this work is to investigate, through inelastic neutron scattering (INS), the vibrational behavior of trehalose and its mixtures with glycerol at different concentration values in order to characterize the changes induced by glycerol on the trehalose hydrogen bonded network. The obtained experimental findings, which are discussed and interpreted in the framework of previous INS, quasi elastic neutron scattering (QENS) and molecular simulation data obtained on trehalose/glycerol mixtures at different concentration and temperature values, will be linked to the different mixtures bioprotectant effectiveness.

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Section: Methodsmentioning

confidence: 99%

Vibrational Properties of Bioprotectant Mixtures of Trehalose and Glycerol

2011

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“…It was shown that the INS technique is particularly useful in the studies on the deformation modes in which the vibrations of hydrogen atoms are involved [24][25][26]. This is due to the large incoherent scattering cross-section of hydrogen and the high amplitudes of these vibrations.…”

Section: Introductionmentioning

confidence: 99%

INS, DFT and temperature dependent IR investigations of dynamical properties of low temperature phase of choline chloride

Pawlukojć

Hetmańczyk

2014

Chemical Physics

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“…Vibrational spectroscopy by inelastic neutron scattering (INS) has, in principle, a natural utility for the investigation of biological systems because of the large sensitivity of neutrons to H in incoherent scattering. Globular proteins [15][16][17][18], collagen and model polypeptides [19,3] and hydration water [4,20] have all been studied with the use of INS, as also have been the structures of interfacial water associated with DNA and gelatin molecules [2]. Only rather qualitative inferences could be drawn from these spectra, namely that at low hydration levels the spectral contribution of hydration water differs strongly from the spectrum of the ice Ih and may be viewed as being more similar to HDA ice, while at high hydration levels the spectrum has a more ice-like appearance.…”

Section: Introductionmentioning

confidence: 99%

Mutual interactions in a ternary protein/bioprotectant/water system

Migliardo

Parker

Eckert

et al. 2018

Vibrational Spectroscopy

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The dynamics of hydration water plays a key role in many biological processes. The activity and function of proteins are strongly affected by the presence of water, which interacts primarily by means of hydrogen bonding. These interactions are examined in this work by a comparison of neutron vibrational spectra (inelastic neutron scattering, INS) of dry lysozyme and hydrated lysozyme at h=0.7 (g of H2 O/g of protein) with those of a lysozyme/water mixture at the same hydration value in the presence of the glass-forming bioprotectant trehalose. A difference spectrum, obtained by subtracting the dry lysozyme spectrum from that of the lysozyme/ water mixture, yields the hydration water spectrum which is compared to the INS spectra of different kinds of ice in order to determine the changes induced by lysozyme on the hydrogen-bonded network of water. An additional comparison is performed by using a doubledifference spectrum obtained by subtracting both the dry lysozyme and the trehalose spectra from the lysozyme/trehalose/water ternary spectrum. The effects of the mutual interactions among the three components, i.e. protein, disaccharide and water, are determined by comparison of the spectra of the dry systems (lysozyme, trehalose) with the difference spectra obtained from subtraction of the dry systems from the binary systems. It is concluded that the interfacial water more strongly affects the intermolecular mode region at low frequencies, whereas the vibrational spectra at high frequencies are more influenced by lysozyme and trehalose.

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Neutron Inelastic Scattering as a High‐Resolution Vibrational Spectroscopy: New Tool for the Study of Protein Dynamics

Cited by 13 publications

References 15 publications

Vibrational Properties of Bioprotectant Mixtures of Trehalose and Glycerol

Vibrational Properties of Bioprotectant Mixtures of Trehalose and Glycerol

INS, DFT and temperature dependent IR investigations of dynamical properties of low temperature phase of choline chloride

Mutual interactions in a ternary protein/bioprotectant/water system

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