Water Dynamics at Protein Interfaces: Ultrafast Optical Kerr Effect Study

Mazur, Kamila; Heisler, Ismael A.; Meech, Stephen R.

doi:10.1021/jp2074539

Cited by 48 publications

(52 citation statements)

References 73 publications

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“…5) in albumin aqueous solution masks the variation of the ''aggregated'' g S , but we can assert the damping constant of hydration water is qualitatively larger than that of bulk water. Since the damping constant g S represents the degree of heterogeneity of the HB environment, large g S of hydration water compared with that of bulk claims that hydration water has a heterogeneous HB network structure, which consists of various HB distances and angles, in good accordance with previous experiments (26,35,37) and simulations (12,14,21,96,97). Such heterogeneous HBs are associated with the distortion of the water HB network, since they involve the distortion of the O...O...O angles from the ideal tetrahedral value.…”

Section: Structural Distortion Of the Water Hydrogen-bond Networksupporting

confidence: 83%

“…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: Structural Distortion Of the Water Hydrogen-bond Networksupporting

confidence: 83%

Section: Introductionmentioning

confidence: 99%

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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“…Two-dimensional infrared spectroscopy with a local carbonyl probe has also determined a modest slowdown factor -approximately 2 -for H-bond dynamics within the hydration layer. 37 Techniques like optical Kerr-effect spectroscopy 38,39 instead probe collective water dynamics (e.g. the relaxation of the system polarization) and have measured slightly larger slowdown factors between 7 and 9, which remain to be explained.…”

Section: Is the Biomolecular Hydration Layer Viscous Or Labile?mentioning

confidence: 99%

Biomolecular hydration dynamics: a jump model perspective

et al. 2013

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The dynamics of water molecules within the hydration shell surrounding a biomolecule can have a crucial influence on its biochemical function. Characterizing their properties and the extent to which they differ from those of bulk water have thus been long-standing questions. Following a tutorial approach, we review the recent advances in this field and the different approaches which have probed the dynamical perturbation experienced by water in the vicinity of proteins or DNA. We discuss the molecular factors causing this perturbation, and describe how they change with temperature. We finally present more biologically relevant cases beyond the dilute aqueous situation. A special focus is on the jump model for water reorientation and hydrogen bond rearrangement.

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“…This feature was unreliable, suggesting that these highly viscous solutions do not fully relax within the timescale of the experiments. A weaker shoulder that appears between 10 and 200 GHz can be explained as 'slow' water diffusing within the protein hydration layer 28,40 .…”

mentioning

confidence: 99%

Terahertz underdamped vibrational motion governs protein-ligand binding in solution

et al. 2014

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Low-frequency collective vibrational modes in proteins have been proposed as being responsible for efficiently directing biochemical reactions and biological energy transport. However, evidence of the existence of delocalized vibrational modes is scarce and proof of their involvement in biological function absent. Here we apply extremely sensitive femtosecond optical Kerr-effect spectroscopy to study the depolarized Raman spectra of lysozyme and its complex with the inhibitor triacetylchitotriose in solution. Underdamped delocalized vibrational modes in the terahertz frequency domain are identified and shown to blue-shift and strengthen upon inhibitor binding. This demonstrates that the ligand-binding coordinate in proteins is underdamped and not simply solvent-controlled as previously assumed. The presence of such underdamped delocalized modes in proteins may have significant implications for the understanding of the efficiency of ligand binding and protein-molecule interactions, and has wider implications for biochemical reactivity and biological function.

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Water Dynamics at Protein Interfaces: Ultrafast Optical Kerr Effect Study

Cited by 48 publications

References 73 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

Biomolecular hydration dynamics: a jump model perspective

Terahertz underdamped vibrational motion governs protein-ligand binding in solution

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