Nuclear magnetic relaxation dispersion in monoclinic lysozyme crystals

Bryant, R. G.; Brown, rd R D; Koenig, SH

doi:10.1016/0301-4622(82)85014-x

Cited by 16 publications

(6 citation statements)

References 10 publications

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“…This is consistent with our 2 H dispersion (Fig. 5) and a previous 1 H dispersion from lysozyme crystals (Bryant et al, 1982), showing that R 1 remains frequency dependent up to 50 MHz at least. At the frequencies (9.2 and 38.7 MHz) of previous 2 H R 1 measurements, R 1 , must therefore include a contribution from motions with correlation times in the nanosecond range.…”

Section: Water Dynamics In Protein Crystalssupporting

confidence: 93%

“…Because a low-frequency plateau is not evident, it would not be meaningful to fit a Lorentzian dispersion function to the data. Indeed, a previously reported water 1 H dispersion from monoclinic lysozyme crystals shows no tendency to level out, even at 10 kHz (Bryant et al, 1982). On the other hand, the R 1 , dispersion observed here is not just the high-frequency tail of a Lorentzian dispersion centered at lower frequency, because the observed frequency dependence is much weaker than inversesquare (cf.…”

Section: Magnetic Relaxation Dispersioncontrasting

confidence: 47%

“…Specifically, we record the orientation dependence of the quadrupole splitting and linewidth in the water 2 H spectrum from a single crystal of bovine pancreatic trypsin inhibitor (BPTI) in the temperature range 6 -50°C. The first water NMR studies of protein crystals used the 1 H isotope (Kru ¨ger and Helcke ´, 1967;Hsi et al, 1976;Bryant et al, 1982). Because of complications with intermolecular cross-relaxation (Hsi and Bryant, 1977) and proton-exchange averaging of the dipolar splitting (Lauterbur et al, 1978), the 2 H isotope has been favored in later work (Lauterbur et al, 1978;Borah and Bryant, 1982;Usha and Wittebort, 1989;Usha et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

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Orientational Order and Dynamics of Hydration Water in a Single Crystal of Bovine Pancreatic Trypsin Inhibitor

Venu

Svensson

Halle

1999

Biophysical Journal

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The orientational order and dynamics of the water molecules in form II crystals of bovine pancreatic trypsin inhibitor (BPTI) are studied by (2)H NMR in the temperature range 6-50 degrees C. From the orientation dependence of the single crystal quadrupole splitting and linewidth, the principal components of the motionally averaged quadrupole interaction tensor and the irreducible linewidth components for the orthorhombic crystal are determined. With the aid of water orientations derived from neutron and x-ray diffraction, it is shown that the NMR data can be accounted for by a small number of highly ordered crystal waters, some of which have residence times in the microsecond range. Most of these specific hydration sites must be located at intermolecular contacts. The surface hydration layer that is also present in dilute solution is likely to be only weakly ordered and would then not contribute significantly to the splitting and linewidth from the protein crystal. To probe water dynamics on shorter time scales, the (2)H longitudinal relaxation dispersion is measured for a polycrystalline BPTI sample. The observed dispersion is dominated by rapidly exchanging deuterons in protein side chains, undergoing restricted rotational motions on a time scale of 10 ns.

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Section: Water Dynamics In Protein Crystalssupporting

confidence: 93%

Section: Magnetic Relaxation Dispersioncontrasting

confidence: 47%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Orientational Order and Dynamics of Hydration Water in a Single Crystal of Bovine Pancreatic Trypsin Inhibitor

Venu

Svensson

Halle

1999

Biophysical Journal

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“…First systematic studies in this field are dating from the sixties [80]. The application of the technique for the study of water-protein interactions and dynamics in protein solutions is extensive up to the present day [92][93][94][95]. The water exchange process between bulk water and molecules trapped in the protein structure can be studied with FC relaxometry [96].…”

Section: Bio-molecules Containing Paramagnetic or Metallic Centers Pmentioning

confidence: 99%

Fast-field-cycling NMR: Applications and instrumentation

Anoardo¹,

Galli²,

Ferrante³

2001

Appl. Magn. Reson.

194

136

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Magnetic field cycling in nuclear magnetic resonance (NMR) experiments has been used since the early days of NMR. Originally such time-dependent magnetic field experiments were motivated to study cross relaxation, spin system thermodynamics and indirect detection of quadrupolar resonance. The first apparatus used mechanical or pneumatic systems to shoot the sample between two magnets, the typical "flying time" being a few hundreds of milliseconds. As a natural evolution of the experimental technique and the need to extend its application to samples with higher relaxation rates, faster magnetic field switching devices were developed during the last years. Special electric networks combined with sophisticated air core magnets allowed one to switch magnetic fields between zero and fields of the order of 0.5 T in a few milliseconds. Today we refer to this new generation of instruments as "fast-field-cycling" devices. The technique has been successfully used during the last years to obtain information on the molecular dynamics and order in different materials, ranging from organic solids, metals, polymers, liquid crystals, porous media to biological systems. At present it is also turning to be an important tool for the design of contrast agents for magnetic resonance imaging. Fast field cycling was mainly oriented to T, relaxometry as a unique technique offering a dynamic window of several decades, ranging from few kilohertz to several megahertz. However, there exist less conventional applications of the technique that can also provide relevant information concerning molecular dynamics, structure and molecular order. In this article we will briefly deal with basic aspects of the technique, its evolution, present-day relevant applications and the last improvements concerning specialized instrumentation.

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“…Unlike the case for 'yh-crystallin, for which these forms retain sufficient rotational mobility to contribute to the monotonic background of the NMRD profiles as do globular proteins, the a-crystallin particles appear sufficiently large, >5 x 104 kD, to be regarded as "microsolids," judging from their slowed rotation. The NMRD profiles become much like those of (irreversibly) immobilized protein (Lindstrom and Koenig, 1974;Bryant et al, 1982Bryant et al, , 1991Beaulieu, 1989;Koenig and Brown, 1991), which, in turn, appear to be models for the NMRD profiles of water protons of most tissue. Indeed, recent ideas on the distinctions between relaxation of water protons in protein solutions and in tissue indicate a transition from liquidto solid-like behavior for relaxation of the macromolecular protons (Koenig and Brown, 1991) that alters the solvent proton NMRD profiles through magnetization transfer across the protein-water interface.…”

Section: Introductionmentioning

confidence: 99%

Intermolecular protein interactions in solutions of calf lens alpha-crystallin. Results from 1/T1 nuclear magnetic relaxation dispersion profiles

Koenig

Brown

Kenworthy

et al. 1992

Biophysical Journal

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From analyses of the magnetic field dependence of 1/T1 (NMRD profiles) of water protons in solutions of calf lens alpha-crystallin at several concentrations, we find two regimes of solute behavior in both cortical and nuclear preparations. Below approximately 15% vol/vol protein concentration, the solute molecules appear as compact globular proteins of approximately 1,350 (cortical) and approximately 1,700 (nuclear) kD. At higher concentrations, the effective solute particle size increases, reversibly, as evidenced by the appearance of spectra-like 14N peaks in the NMRD profiles and a change in the field and temperature dependence of 1/T1. At these higher concentrations, the profiles are very similar to those of calf gamma II-crystallin, a crystallin that undergoes an analogous transition near approximately 15% protein (Koenig, S. H., C.F. Beaulieu, R. D. Brown III, and M. Spiller, 1990. Biophys. J. 57:461-469). By comparison with recent analyses of NMRD results for solutions of immobilized proteins as models for the transition from protein solutions to tissue (Koenig, S. H., and R. D. Brown III. 1991. Prog. NMR Spectr. 22:487-567), we argue that alpha-crystallin solute behaves as aggregates approximately greater than 50,000 kD as protein concentration is progressively increased above 15%. Finally, the concentration dependence of the NMRD profiles of alpha- and gamma II-crystallin can readily explain recent osmotic pressure data, in particular the intersection of the respective pressure curves at approximately 23% vol/vol (Vérétout, F., and A. Tardieu. 1989. Eur. Biophys. J. 17:61-68).

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Nuclear magnetic relaxation dispersion in monoclinic lysozyme crystals

Cited by 16 publications

References 10 publications

Orientational Order and Dynamics of Hydration Water in a Single Crystal of Bovine Pancreatic Trypsin Inhibitor

Orientational Order and Dynamics of Hydration Water in a Single Crystal of Bovine Pancreatic Trypsin Inhibitor

Fast-field-cycling NMR: Applications and instrumentation

Intermolecular protein interactions in solutions of calf lens alpha-crystallin. Results from 1/T1 nuclear magnetic relaxation dispersion profiles

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