More Is Different: Experimental Results on the Effect of Biomolecules on the Dynamics of Hydration Water

Comez, Lucia; Lupi, Laura; Morresi, Assunta; Paolantoni, Marco; Sassi, Paola; Fioretto, D.

doi:10.1021/jz400360v

Cited by 73 publications

(104 citation statements)

References 36 publications

(64 reference statements)

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“…Molecular dynamics (MD) simulations (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22) and other experimental approaches (23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37) have revealed the protein is surrounded by dynamically retarded hydration water, with the innermost shell having a density higher than that of bulk water. However, even today, experimentally characterizing the dynamics and the structure of the water HB network in this hydration shell is challenging, because the water-water HB lifetime is very short (typically 1 ps) (38).…”

Section: Introductionmentioning

confidence: 99%

“…However, even today, experimentally characterizing the dynamics and the structure of the water HB network in this hydration shell is challenging, because the water-water HB lifetime is very short (typically 1 ps) (38). To observe directly the HB dynamics and structure fluctuating at subpicosecond to picosecond timescales, depolarized light scattering (DLS) (33,34), optical Kerr effect (OKE) spectroscopy (35), incoherent neutron scattering (INS) spectroscopy (36), and Brillouin spectroscopy (37) were developed, but they all have experimental limitations. DLS and OKE probe weak second-order optical processes, and INS and Brillouin spectroscopy require isotopic substitution, which may alter the native water HB network, if only weakly.…”

Section: Introductionmentioning

confidence: 99%

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Hydrogen Bond Network of Water around Protein Investigated with Terahertz and Infrared Spectroscopy

Shiraga

Ogawa

Kondo

2016

Biophysical Journal

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The dynamical and structural properties of water at protein interfaces were characterized on the basis of the broadband complex dielectric constant (0.25 to 400 THz) of albumin aqueous solutions. Our analysis of the dielectric responses between 0.25 and 12 THz first revealed hydration water with retarded reorientational dynamics extending~8.5 Å (corresponding to three to four layers) out from the albumin surface. Second, the number of nonhydrogen-bonded water was decreased in the presence of the albumin solute, indicating protein inhibits the fragmentation of the water hydrogen-bond network. Finally, water molecules at the albumin interface were found to form a distorted hydrogen-bond structure due to topological and energetic disorder of the protein surface. In addition, the intramolecular O-H stretching vibration of water (~100 THz), which is sensitive to hydrogen-bond environment, pointed to a trend that hydration water has a larger population of strongly hydrogen-bonded water molecules compared with that of bulk water. From these experimental results, we concluded that the ''strengthened'' water hydrogen bonds at the protein interface dynamically slow down the reorientational motion of water and form the less-defective hydrogen-bond network by inhibiting the fragmentation of water-water hydrogen bonds. Nevertheless, such a strengthened water hydrogen-bond network is composed of heterogeneous hydrogen-bond distances and angles, and thus characterized as structurally ''distorted.''

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Hydrogen Bond Network of Water around Protein Investigated with Terahertz and Infrared Spectroscopy

Shiraga

Ogawa

Kondo

2016

Biophysical Journal

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“…[14][15][16] These heterogeneously polarized, heterogeneously compressed, [17][18][19] and potentially mutually frustrated interfacial water domains merge into an interfacial sub-ensemble involving several hundreds of water molecules, with its properties quite distinct from the bulk. 20,21 The bulk perspective does not apply just to the protein part of the thermal bath, but to the hydration shell as well.…”

Section: Introductionmentioning

confidence: 99%

Protein electron transfer: Dynamics and statistics

Matyushov

2013

The Journal of Chemical Physics

121

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A statistical-mechanical analysis on the hypermobile water around a large solute with high surface charge density J. Chem. Phys. 130, 014707 (2009) Electron transfer between redox proteins participating in energy chains of biology is required to proceed with high energetic efficiency, minimizing losses of redox energy to heat. Within the standard models of electron transfer, this requirement, combined with the need for unidirectional (preferably activationless) transitions, is translated into the need to minimize the reorganization energy of electron transfer. This design program is, however, unrealistic for proteins whose active sites are typically positioned close to the polar and flexible protein-water interface to allow inter-protein electron tunneling. The high flexibility of the interfacial region makes both the hydration water and the surface protein layer act as highly polar solvents. The reorganization energy, as measured by fluctuations, is not minimized, but rather maximized in this region. Natural systems in fact utilize the broad breadth of interfacial electrostatic fluctuations, but in the ways not anticipated by the standard models based on equilibrium thermodynamics. The combination of the broad spectrum of static fluctuations with their dispersive dynamics offers the mechanism of dynamical freezing (ergodicity breaking) of subsets of nuclear modes on the time of reaction/residence of the electron at a redox cofactor. The separation of time-scales of nuclear modes coupled to electron transfer allows dynamical freezing. In particular, the separation between the relaxation time of electro-elastic fluctuations of the interface and the time of conformational transitions of the protein caused by changing redox state results in dynamical freezing of the latter for sufficiently fast electron transfer. The observable consequence of this dynamical freezing is significantly different reorganization energies describing the curvature at the bottom of electron-transfer free energy surfaces (large) and the distance between their minima (Stokes shift, small). The ratio of the two reorganization energies establishes the parameter by which the energetic efficiency of protein electron transfer is increased relative to the standard expectations, thus minimizing losses of energy to heat. Energetically efficient electron transfer occurs in a chain of conformationally quenched cofactors and is characterized by flattened free energy surfaces, reminiscent of the flat and rugged landscape at the stability basin of a folded protein.

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“…[13][14][15] The influence of small and large molecules on the surrounding solvent molecules has been described in terms of both destructuring/restructuring effects on the whole HB assembly of water molecules 16 and change in the local dynamics of the solvent at different chemical sites. [17][18][19][20] Recently, we used oligosaccharide based hydrogels as model systems to study the effect on the HB dynamics of water [21][22][23][24] of two factors, i.e. (i) the nano-scale confinement of water and (ii) the presence of hydrophobic/hydrophilic portions at the interface with the solvent.…”

Section: Introductionmentioning

confidence: 99%

“…IR and Raman spectroscopy can be conveniently employed for the quantitative evaluation of the extent of perturbation on water organization due to the combination of confinement effects 3,4,[6][7][8] and interactions with hydrophobic/ hydrophilic portions of the confining polymeric matrix. [15][16][17]19 In the past few years, it was shown that the combination of UV-Raman scattering experiments and FT-IR spectroscopy is a simple strategy to separate the spectral response arising from the polymer matrix and the water molecules. [21][22][23][24] The separate analysis of the vibrational dynamics associated with confined water molecules and the polymer skeleton thus provides new insights into the interplay of different types of HB interactions that coexist in hydrogel phases.…”

Section: Introductionmentioning

confidence: 99%

Vibrational signatures of the water behaviour upon confinement in nanoporous hydrogels

Rossi

Venuti

Punta

et al. 2016

Phys. Chem. Chem. Phys.

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The fundamental question of how the reorganization of the hydrogen-bond (HB) network of water is influenced by the combination of nano-confinement and hydrophobic/hydrophilic solvation effects is addressed here using a spectroscopic study of water absorbed in a model, pH-sensitive polysaccharide hydrogel. The effects of temperature, hydration level and pH on the vibrational dynamics associated with the water molecules and the polymer skeleton are disentangled and analysed by a complementary and combined use of UV-Raman scattering and IR spectroscopy. The experimental data give evidence that the solvation effects in the hydrogel matrix are essentially dominated by the hydration of more hydrophobic parts of the polymer network, while the effect of pH on the HB reorganization of confined water molecules is found to be similar to that induced by cooling of the system. A tentative explanation of these results has been provided in terms of interplay between different kinds of interactions, i.e. hydrophobic vs. hydrophilic.

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More Is Different: Experimental Results on the Effect of Biomolecules on the Dynamics of Hydration Water

Cited by 73 publications

References 36 publications

Hydrogen Bond Network of Water around Protein Investigated with Terahertz and Infrared Spectroscopy

Hydrogen Bond Network of Water around Protein Investigated with Terahertz and Infrared Spectroscopy

Protein electron transfer: Dynamics and statistics

Vibrational signatures of the water behaviour upon confinement in nanoporous hydrogels

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