Nuclear Magnetic Resonance of Single Crystals of D2O Ice

Waldstein, Peter; Rabideau, Sherman W.; Jackson, Jasper A.

doi:10.1063/1.1725740

Cited by 148 publications

(34 citation statements)

References 11 publications

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“…The fact that these values agree well with reported e 2 Qq/h values, 213 and 216 kHz, and 77 = 0.1, for the rigid water molecules in D20-ice [13] implies that the greater part of the interlayerwater freezes below 200 K, where the swelling at the centre of the spectrum shows that some slow motion is occurring even at 175 K. Upon heating, the 2 H spectrum was drastically sharpened around 220 K. At 260 K, the spectrum shows a well-defined structure again. We then eliminated the possibility that a combination of two or more motions of D 2 0 molecules might explain the observed spectral narrowing by determining the 2 H NMR relaxation time (T\).…”

Section: Resultssupporting

confidence: 81%

NMR Studies on the Dynamics of Intercalated Water in Li-saponite

Ishimaru

Ikeda

1997

Zeitschrift Für Naturforschung A

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The dynamics of intercalated water molecules in Li-saponite was studied by measurement of solid state 2H and 7Li NMR spectra and of the 2H spin-lattice relaxation time at 175 ~ 350 K. Only a single component was observed in the 2H spectra above 260 K, suggesting that the water hydrogens rapidly exchange their positions between various distinct environments. Analysis of the observed spectra suggests that the water molecules possess C2 rotational freedom at around 260 K and that the hydration shell around Li+ cations is highly symmetrical in the same temperature region

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Section: Resultssupporting

confidence: 81%

NMR Studies on the Dynamics of Intercalated Water in Li-saponite

Ishimaru

Ikeda

1997

Zeitschrift Für Naturforschung A

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“…4B. This broad 2 H tensor has a quadrupolar splitting of about 185 kHz, which is slightly smaller than the values reported for immobilized D 2 O quadrupolar coupling of 216 kHz for hexagonal ice or 192 kHz for polycrystalline ice (35,36). The red spectrum in Fig.…”

mentioning

confidence: 59%

Protein–ice interaction of an antifreeze protein observed with solid-state NMR

Siemer

Huang

McDermott

2010

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

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NMR on frozen solutions is an ideal method to study fundamental questions of macromolecular hydration, because the hydration shell of many biomolecules does not freeze together with bulk solvent. In the present study, we present previously undescribed NMR methods to study the interactions of proteins with their hydration shell and the ice lattice in frozen solution. We applied these methods to compare solvent interaction of an ice-binding type III antifreeze protein (AFP III) and ubiquitin a non-ice-binding protein in frozen solution. We measured 1 H-1 H cross-saturation and cross-relaxation to provide evidence for a molecular contact surface between ice and AFP III at moderate freezing temperatures of −35°C. This phenomenon is potentially unique for AFPs because ubiquitin shows no such cross relaxation or cross saturation with ice. On the other hand, we detected liquid hydration water and strong water-AFP III and water-ubiquitin cross peaks in frozen solution using relaxation filtered 2 H and HETCOR spectra with additional 1 H-1 H mixing. These results are consistent with the idea that ubiquitin is surrounded by a hydration shell, which separates it from the bulk ice. For AFP III, the water cross peaks indicate that only a portion of its hydration shell (i.e., at the ice-binding surface) is in contact with the ice lattice. The rest of AFP III's hydration shell behaves similarly to the hydration shell of non-ice-interacting proteins such as ubiquitin and does not freeze together with the bulk water.hydration shell | type III AFP | ice binding | water solute interaction A ntifreeze proteins (AFPs) can be found in a variety of coldadapted organisms including bacteria, plants, insects, and fish (1). AFPs lower the freezing point of a given solution below its melting point, a process called thermal hysteresis. This thermal hysteresis is thought to result from the strong binding of the AFP to the surface of ice crystals making their further growth energetically unfavorable (2, 3). One of the most intensely studied classes of AFPs is the type III AFPs from the ocean pound. In particular the HPLC-12 isoform (in the following just termed AFP III), was studied with X-ray crystallography (4), NMR (5, 6), mutagenesis (4,7,8), and molecular dynamics (9). These studies showed that the ice-binding site of AFP III is a flat surface formed by predominantly nonpolar residues (5, 8), which is remarkable because the solvent accessible surface of other soluble proteins like ubiquitin are predominantly polar. There have been limited opportunities to study the water molecules at the ice-binding surface of AFPs, although recent computational and sub-angstrom X-ray structures indicate ordered water molecules at the ice-binding surface (9, 10).Ice, with its very slow 1 H spin-lattice relaxation rate (R 1 ) and very fast spin-spin relaxation rate (R 2 ), is relatively difficult to study with NMR. Measurements of relaxation rates of ice showed that R 2 is on the order of 10 6 s −1 and R 1 on the order of 10at a temperatures of about 260 K...

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“…The quadrupole coupling interaction is sometimes neglected for simulations of ,H-ESEEM because it is usually small. Waldstein et al (25) reported that e"qQ and I q I of DzO ice were 0.215 MHz and 0.1, respectively, by NMR. The quadrupole coupling constant of deuterium in this system is 0.37 MHz, which is slightly larger than that in D,O ice.…”

Section: H-eseem Of Gd-lthamentioning

confidence: 98%

Solvate structures in water‐methanol solutions of MRI contrast agents: Electron spin echo envelope modulation in gadolinium chelates

Clarkson

Hwang

Belford

1993

Magnetic Resonance in Med

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Electron Spin Echo Envelope Modulation (ESEEM) data are reported for three gadolinium (III) chelates, Gd-EDTA, Gd-DTPA, and Gd-TTHA, in frozen D2O/CH3OD glasses. This series includes Gd-DTPA, an MRI contrast agent that is in clinical use. Three-pulse electron spin echo modulation patterns can be modeled to yield geometrical information; e.g., distances and numbers of Gd+3-OD interactions. Interpreted by a spherical shell model, the data for Gd-TTHA are accounted for by Gd+3 surrounded by seven deuterons at an effective distance of 3.9 A. We attribute these deuterons to second-coordination sphere solvent molecules, since it is likely that Gd+3 is fully coordinated by a TTHA ligand. For analysis of ESEEM from Gd-EDTA and Gd-DTPA, the second-sphere structures of Gd-EDTA, Gd-DTPA, and Gd-TTHA are assumed equivalent. 2H-ESEEM from inner-sphere solvent molecules gives the effective distance between deuterons and Gd+3 to be approximately 2.7 A for the inner-sphere water in both EDTA and DTPA complexes. The results of simulations also give the isotropic hyperfine and quadrupole coupling constants for solvent deuterium in these systems. Possible sources of error in the determination of r and q by this method are discussed.

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Nuclear Magnetic Resonance of Single Crystals of D2O Ice

Cited by 148 publications

References 11 publications

NMR Studies on the Dynamics of Intercalated Water in Li-saponite

NMR Studies on the Dynamics of Intercalated Water in Li-saponite

Protein–ice interaction of an antifreeze protein observed with solid-state NMR

Solvate structures in water‐methanol solutions of MRI contrast agents: Electron spin echo envelope modulation in gadolinium chelates

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