Proton nuclear magnetic resonance relaxation of water on lysozyme powders

Hilton, Bruce D.; Hsi, E.; Bryant, R. G.

doi:10.1021/ja00468a017

Cited by 47 publications

(21 citation statements)

References 7 publications

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“…In addition, it must be appreciated that this sample is not completely hydrated; the normal complement of nonfreezable water associated with lysozyme is approximately twice the water content of the sample used (13,27). There is good evidence that increasing water content leads to increased motion in the water adsorbed (21); therefore, the present case overestimates the correlation time for the water present in a fully hydrated protein sample. We may conclude then that the correlation time for the reorientation of the interproton vector of the water molecule changes by less than a factor of 100 in going from the liquid to an adsorbed state where the protein is constrained not to rotate.…”

Section: (D)mentioning

confidence: 77%

“…A set of measurements at different pulse widths to vary MW(O) and Mp(O) provides a means of extracting the basic relaxation rates. Rlp is small, even set to zero in an earlier treatment (21), so that the precision obtainable by extracting it together with the other two rates is poor. An alternative procedure is to measure RIP directly in a protein system hydrated to the desired level with D20, then extract RIw and RT directly from the nonexponential water proton relaxation curves on similar samples hydrated with H20.…”

Section: (D)mentioning

confidence: 99%

“…The assertion that intermolecular or cross-relaxation effects often dominate water proton NMR relaxation in protein systems is well-supported (20)(21)(22). The simplest and perhaps the most direct support is the observation that the water proton longitudinal relaxation is not described by a single time constant but by a sum of exponential time constants.…”

mentioning

confidence: 98%

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Dynamical deductions from nuclear magnetic resonance relaxation measurements at the water-protein interface

Bryant¹,

Shirley²

1980

Biophysical Journal

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Nuclear magnetic resonance (NMR) measurements provide both structural and dynamical information about the molecules in which nuclear resonances are observed. This manuscript addresses NMR relaxation of water protons in protein powder systems. Inclusion of magnetic communication between the water proton spins and protein proton spins leads to a clearer view of water molecule dynamics at the protein surface than has been previously available. We conclude that water molecule motion at the protein surface is somewhat slower than in the solute free solvent, but it is orders of magnitude faster than motions in a rigid ice lattice even in samples hydrated to levels well below what is generally thought to be the full hydration complement of the protein. The NMR relaxation data on lysozyme powders support a model that leaves adsorbed water very fluid at the protein surface with reorientational correlation times for the water shorter than nanoseconds.

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Section: (D)mentioning

confidence: 77%

Section: (D)mentioning

confidence: 99%

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Dynamical deductions from nuclear magnetic resonance relaxation measurements at the water-protein interface

Bryant¹,

Shirley²

1980

Biophysical Journal

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“…[1] has been observed in other polymeric systems (8,9), no detailed understanding of the underlying changes in molecular dynamics with MC, responsible for the observed effects, has been reported.…”

Section: Resultsmentioning

confidence: 99%

NMR and Monte Carlo Simulation Studies of Water Adsorption Dynamics

Lam

Peemoeller

Chen

2002

Journal of Colloid and Interface Science

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“…24 According to this model, water is found in one of five sites. A site is characterized entirely by the number of hydrogen bonds between a particular water molecule and other water molecules.…”

Section: Nuclear Spin Relaxationmentioning

confidence: 99%

Hydration study of homopolypeptides by ²H NMR

Peemoeller¹,

Stanley²,

Macmillan³

et al. 2007

Biopolymers

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Deuteron T(1) and T(2) was studied as a function of hydration in homopolyglycine (PG) and homopolyproline (PP). Water deuteron relaxation rates in PG conform to a hydration model involving two types of primary hydration sites where water is directly bonded to the polymer. Once these sites are filled, additional water only bonds to water molecules at the primary sites and in so doing affect their dynamics. PP exhibits an anomalous T(1) and T(2) hydration dependence which has been interpreted in terms of a cooperative water molecule-PP molecule helical conformational rearrangement which occurs once a certain hydration level is reached. The proposal of a water-PP structure is tested using molecular dynamics simulations.

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Proton nuclear magnetic resonance relaxation of water on lysozyme powders

Cited by 47 publications

References 7 publications

Dynamical deductions from nuclear magnetic resonance relaxation measurements at the water-protein interface

Dynamical deductions from nuclear magnetic resonance relaxation measurements at the water-protein interface

NMR and Monte Carlo Simulation Studies of Water Adsorption Dynamics

Hydration study of homopolypeptides by ²H NMR

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Proton nuclear magnetic resonance relaxation of water on lysozyme powders

Cited by 47 publications

References 7 publications

Dynamical deductions from nuclear magnetic resonance relaxation measurements at the water-protein interface

Dynamical deductions from nuclear magnetic resonance relaxation measurements at the water-protein interface

NMR and Monte Carlo Simulation Studies of Water Adsorption Dynamics

Hydration study of homopolypeptides by 2H NMR

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Hydration study of homopolypeptides by ²H NMR