Linearity between Structural Correlation Length and Correlated-Proton Raman Intensity from Amorphous Ice and Supercooled Water up to Dense Supercritical Steam

Walrafen, G. E.; Chu, Y. C.

doi:10.1021/j100028a025

Cited by 135 publications

(154 citation statements)

References 2 publications

(5 reference statements)

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“…The ratio of the intensities of the first two components in bulk water is sensitive to water hydrogen-bond network rearrangements caused by temperature and pressure. For example, changes in the 3,250͞ 3,450 cm Ϫ1 intensity ratio vs. temperature correlate well with changes in the bulk water radial distribution function measured by x-ray and neutron scattering (22).…”

Section: Discussionmentioning

confidence: 54%

“…3a and 4). The OH spectra from partially dehydrated collagen correspond to cooled or even supercooled water (22) rather than the heated one.…”

Section: Discussionmentioning

confidence: 99%

“…It has been suggested that the 3,250 cm Ϫ1 and 3,450 cm Ϫ1 bands are associated with different modes of OOH vibrations in the hydrogen-bonded network of water molecules while the 3,600 cm Ϫ1 band is due to vibrations in nonhydrogen-bonded OOH (e.g., see ref. 22 and references therein). The ratio of the intensities of the first two components in bulk water is sensitive to water hydrogen-bond network rearrangements caused by temperature and pressure.…”

Section: Discussionmentioning

confidence: 99%

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Raman spectral evidence for hydration forces between collagen triple helices

Leikin

Parsegian²,

Yang³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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159

127

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Hydration forces are thought to result from the energetic cost of water rearrangement near macromolecular surfaces. Raman spectra, collected on the same collagen samples on which these forces were measured, reveal a continuous change in water hydrogen-bonding structure as a function of separation between collagen triple helices. The varying spectral parameters track the force-distance curve. The energetic cost of water ''restructuring,'' estimated from the spectra, is consistent with the measured energy of intermolecular interaction. These correlations support the idea that the change in water structure underlies the exponentially varying forces seen in this system at least over the 13-18-Å range of interaxial separations.The structure of water surrounding collagen has been studied by a wide variety of techniques and is considered a paradigm for protein hydration. It is commonly accepted that at least some water in collagen fibers differs from bulk, ambient water. Within the most simple scheme, this interstitial water is separated into two distinct classes-tightly bound and ''free'' or bulk-like (1, 2). More elaborate models imagine three or even more fractions (3-8). Tightly bound waters are believed to stabilize the triple helix by participating in the H-bond backbone (see ref. 9 for a review). In a larger context, however, the specific role of water in collagen assembly, structure and stability is still an open question.New insights into the structure and the role of water near collagen come from the high-resolution x-ray structure of a collagen-like peptide (10, 11). Malleable clusters and chains of H-bonded waters form a complex network connected to polar side chains and to backbone carbonyls on the peptide triple helices. The uncharged helices do not show any direct contacts; water directly mediates the interaction between them.This interpretation of the x-ray results correlates well with the picture that has emerged from direct measurement of force-distance curves between triple helices. It has been argued that the measured short-range repulsion, which prevents collagen molecules from coming too close to each other, originates from the energetic cost of removal of the interstitial water (12-14). The longer-range attraction, which prevents the molecules from coming too far apart and which induces self-assembly of collagen fibers from solution, appears to be associated with formation of hydrogen bonded water bridges at specific recognition sites (13). The arguments, however, have been based so far on the process of elimination of other explanations for the observed forces, rather than on direct observation of changes in water structure.The present study establishes more explicit connection between forces and water structure by observing Raman spectra from the same samples on which osmotic stress force measurements have been made. We analyze the changes in the OOH and NOH vibrational bands measured in the 3,100-3,800-cm Ϫ1 range as a function of separation between collagen triple helices and correlat...

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Section: Discussionmentioning

confidence: 54%

“…3a and 4). The OH spectra from partially dehydrated collagen correspond to cooled or even supercooled water (22) rather than the heated one.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Raman spectral evidence for hydration forces between collagen triple helices

Leikin

Parsegian²,

Yang³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

159

127

View full text Add to dashboard Cite

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“…But since the contour of the O-H profile is broad and complex, the most reasonable way to get information about the effect of T, as well as the confinement, on the structural arrangements of water is to perform a deconvolution of the Raman OH band into Gaussian components. Actually, in a recent paper, 22 we studied the influence of T as well as the fine size effects on similar samples by deconvoluting the O-H stretching region into four symmetrical profiles in accordance with an interesting model proposed by Walrafen et al 14,15 for bulk H 2 O some years ago. Essentially, the interpretation formulated in our previous work has been partially used here, but with a further and deeper refinement of the aforementioned subbands assignment, having added a new contribution at ¾3020 cm 1 , properly discussed in the framework proposed by Li et al 23 Hence, we best-fitted all the spectra, starting from bulk water passing to the confined sample, both in the case of native and silanised GelSil glass, into five Gaussians, each of them assigned to a particular O-H vibration related to the specific interaction with the absorbing silica substrate.…”

Section: Resultsmentioning

confidence: 98%

A new insight on the hydrogen bonding structures of nanoconfined water: a Raman study

Crupi

Interdonato

Longo

et al. 2007

J Raman Spectroscopy

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Water adsorbed in nanoporous silica glass has been investigated by Raman spectroscopy. The analysis was performed as a function of temperature (from +5 to +75°C), pore diameter (25 and 75Å) and by changing the nature of the substrate (from hydrophilic to hydrophobic) in order to understand the role played on the dynamic peculiarities of water arrangements both by the bare geometrical confinement and the specific interaction with surface. The experimental spectra, collected in the intra-molecular O-H stretching vibrational region, have been decomposed into a sum of sub-bands, representing water molecule arrangements with different types of hydrogen bonding. Hence, we gave a quantitative picture of the temperature and confinement effects on the connectivity pattern.

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“…We observe two bands in the power spectra of water at about 2 and 8 THz. The lower frequency band has been interpreted [42,43] as corresponding to the O· · · O· · · O bending mode from triplets of hydrogen-bonded water molecules and the higher frequency band as O· · · O stretching mode between pairs of hydrogen-bonded water molecules. Turning to the hydration water, the results plotted in Figure 2(a) reveal a clear blue shift in S O (ω) for the band corresponding to the O· · · O· · · O bending for water.…”

Section: Vacf Power Spectramentioning

confidence: 99%

Analysis of Water and Hydrogen Bond Dynamics at the Surface of an Antifreeze Protein

Gnanasekaran

Leitner

2012

Journal of Atomic, Molecular, and Optical Physics

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We examine dynamics of water molecules and hydrogen bonds at the water-protein interface of the wild-type antifreeze protein from spruce budworm Choristoneura fumiferana and a mutant that is not antifreeze active by all-atom molecular dynamics simulations. Water dynamics in the hydration layer around the protein is analyzed by calculation of velocity autocorrelation functions and their power spectra, and hydrogen bond time correlation functions are calculated for hydrogen bonds between water molecules and the protein. Both water and hydrogen bond dynamics from subpicosecond to hundred picosecond time scales are sensitive to location on the protein surface and appear correlated with protein function. In particular, hydrogen bond lifetimes are longest for water molecules hydrogen bonded to the ice-binding plane of the wild type, whereas hydrogen bond lifetimes between water and protein atoms on all three planes are similar for the mutant.

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Linearity between Structural Correlation Length and Correlated-Proton Raman Intensity from Amorphous Ice and Supercooled Water up to Dense Supercritical Steam

Cited by 135 publications

References 2 publications

Raman spectral evidence for hydration forces between collagen triple helices

Raman spectral evidence for hydration forces between collagen triple helices

A new insight on the hydrogen bonding structures of nanoconfined water: a Raman study

Analysis of Water and Hydrogen Bond Dynamics at the Surface of an Antifreeze Protein

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