Neutron scattering evidence of a boson peak in protein hydration water

Paciaroni, Alessandro; Bizzarri, Anna Rita; Cannistraro, Salvatore

doi:10.1103/physreve.60.r2476

Cited by 58 publications

(67 citation statements)

References 25 publications

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“…Correspondingly, it is possible that the increase in intensity at ∼20 cm −1 in the protein-ligand sample also reflects localized protein, intramolecular interactions that accompany ligand binding. The 20 cm −1 experimental mode may be associated with delocalized side-chain fluctuations and has been uncovered in numerous protein investigations [37][38][39].…”

Section: Hinge-bending Mode and Protein Intramolecular Interactionsmentioning

confidence: 93%

THz time scale structural rearrangements and binding modes in lysozyme-ligand interactions

Woods

2014

J Biol Phys

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Predicting the conformational changes in proteins that are relevant for substrate binding is an ongoing challenge in the aim of elucidating the functional states of proteins. The motions that are induced by protein-ligand interactions are governed by the protein global modes. Our measurements indicate that the detected changes in the global backbone motion of the enzyme upon binding reflect a shift from the large-scale collective dominant mode in the unbound state towards a functional twisting deformation that assists in closing the binding cleft. Correlated motion in lysozyme has been implicated in enzyme function in previous studies, but detailed characterization of the internal fluctuations that enable the protein to explore the ensemble of conformations that ultimately foster largescale conformational change is yet unknown. For this reason, we use THz spectroscopy to investigate the picosecond time scale binding modes and collective structural rearrangements that take place in hen egg white lysozyme (HEWL) when bound by the inhibitor (NAG) 3 . These protein thermal motions correspond to fluctuations that have a role in both selecting and sampling from the available protein intrinsic conformations that communicate function. Hence, investigation of these fast, collective modes may provide knowledge about the mechanism leading to the preferred binding process in HEWL-(NAG) 3 . Specifically, in this work we find that the picosecond time scale hydrogen-bonding rearrangements taking place in the protein hydration shell with binding modify the packing density within the hydrophobic core on a local level. These localized, intramolecular contact variations within the protein core appear to facilitate the large cooperative movements within the interfacial region separating the α-and β-domain that mediate binding. The THz time-scale fluctuations identified in the protein-ligand system may also reveal a molecular mechanism for substrate recognition.

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Section: Hinge-bending Mode and Protein Intramolecular Interactionsmentioning

confidence: 93%

THz time scale structural rearrangements and binding modes in lysozyme-ligand interactions

Woods

2014

J Biol Phys

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“…Even though experimental evidence has been provided in the past for the presence of a Boson peak in HDA ice 152 , more recent neutron time-of-flight and backscattering spectroscopy results seem to rule out this possibility 153 . On the other hand, a Boson peak has been found in experiments on and simulations of protein hydration water 154,155 , simulations of supercooled water 156 and supercooled confined water 134 .…”

Section: The Boson Peakmentioning

confidence: 99%

X-ray and Neutron Scattering of Water

et al. 2016

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International audienceThis review article focuses on the most recent advances in X-ray and neutron scattering studies of water structure, from ambient temperature to the deeply supercooled and amorphous states, and of water diffusive and collective dynamics, in disparate thermodynamic conditions and environments. In particular, the ability to measure X-ray and neutron diffraction of water with unprecedented high accuracy in an extended range of momentum transfers has allowed the derivation of detailed O–O pair correlation functions. A panorama of the diffusive dynamics of water in a wide range of temperatures (from 400 K down to supercooled water) and pressures (from ambient up to multiple gigapascals) is presented. The recent results obtained by quasi-elastic neutron scattering under high pressure are compared with the existing data from nuclear magnetic resonance, dielectric and infrared measurements, and modeling. A detailed description of the vibrational dynamics of water as measured by inelastic neutron scattering is presented. The dependence of the water vibrational density of states on temperature and pressure, and in the presence of biological molecules, is discussed. Results about the collective dynamics of water and its dispersion curves as measured by coherent inelastic neutron scattering and inelastic X-ray scattering in different thermodynamic conditions are reported

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“…The FSDC appears to be of importance also for hydrated proteins; the phenomenon can be observed not only for confined water but also for hydrated biosystems such as proteins, 17,[19][20][21][22][23][24] where the Boson peak has been also observed. 16,25 For clarity we note that, besides these many signatures on the FSDC importance in material science, it has been questioned especially in the case of the water-protein systems. 26,27 Recent approaches to estimating T L have stressed the fundamental importance of the crossover across various subfields of material science.…”

Section: Introductionmentioning

confidence: 99%

The influence of water on protein properties

Mallamace

Baglioni

Corsaro

et al. 2014

The Journal of Chemical Physics

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The "dynamic" or "glass" transition in biomolecules is as important to their functioning as the folding process. This transition occurs in the low temperature regime and has been related to the onset of biochemical activity that is dependent on the hydration level. This protein transition is believed to be triggered by the strong hydrogen bond coupling in the hydration water. We study the vibrational bending mode and measure it using Fourier Transform Infrared spectroscopy. We demonstrate that at the molecular level the hydration water bending mode bonds the C=O and N-H peptide groups, and find that the temperature of the "dynamic" protein transition is the same as the fragile-to-strong dynamic transition in confined water. The fragile-to-strong dynamic transition in water governs the nature of the H bonds between water and peptides and appears to be universal in supercooled glass-forming liquids.

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Neutron scattering evidence of a boson peak in protein hydration water

Cited by 58 publications

References 25 publications

THz time scale structural rearrangements and binding modes in lysozyme-ligand interactions

THz time scale structural rearrangements and binding modes in lysozyme-ligand interactions

X-ray and Neutron Scattering of Water

The influence of water on protein properties

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