Magnetization transfer, cross‐relaxation, and chemical exchange in rotationally immobilized protein gels

Zhou, Dawei; Bryant, Robert G.

doi:10.1002/mrm.1910320607

Cited by 31 publications

(23 citation statements)

References 35 publications

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“…Our findings on the modification of the water off-resonance MT dispersion curves with solvent composition are in agreement with previous reports (e.g., see Refs. [15][16][17].…”

Section: Discussionmentioning

confidence: 98%

On the Importance of Exchangeable NH Protons in Creatine for the Magnetic Coupling of Creatine Methyl Protons in Skeletal Muscle

Kruiskamp

Nicolay

2001

Journal of Magnetic Resonance

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“…Our findings on the modification of the water off-resonance MT dispersion curves with solvent composition are in agreement with previous reports (e.g., see Refs. [15][16][17].…”

Section: Discussionmentioning

confidence: 98%

On the Importance of Exchangeable NH Protons in Creatine for the Magnetic Coupling of Creatine Methyl Protons in Skeletal Muscle

Kruiskamp

Nicolay

2001

Journal of Magnetic Resonance

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“…There is a major difference between these techniques and the one reported here. In multi-dimensional NMR and relaxation dispersion, the amount of the bulk water allowed to be visible can be strategically controlled, e g , by solvent suppression (14) and by partial deuterium (15,(35)(36), or I7O substitution (16). In the present study, water protons, except for the indirect saturation and occasionally freezing below the phase transition temperature, are left untouched.…”

Section: Discussionmentioning

confidence: 99%

Temperature dependence and phase transition of proton relaxation of hydrated collagen in intact beef tendon specimens via cross‐relaxation spectroscopy

Tzou¹,

Lee²,

Yeung³

1997

Magnetic Resonance in Med

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The role of water of hydration in proton relaxation in tissues as exemplified by hydrated collagen in beef tendon was studied as a function of temperature from -40 degrees to 37 degrees C by using cross-relaxation spectroscopy. Experimental data were fitted to a simple binary spin-bath model. The outcome of this procedure allows the construction of a semi-quantitative depiction of proton relaxation in a heterogeneous system and its change as one of the water fractions freezes at about -10 to -20 degrees C, a transition observed by NMR and confirmed independently by differential scanning calorimetry. Such physical depiction provides a crude but insightful interpretation of the role "bound" water plays in proton relaxation. This may be important in shedding light on the mechanism of tissue relaxation and its role in MRI diagnosis, particularly for those diseases such as liver cirrhosis where the water-macromolecular interaction plays a prominent role.

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“…In highly hydrated protein gels, B is found to be 0.5, corresponding to two-dimensional defect diffusion (Zhou and Bryant, 1994).…”

Section: Magnetic Relaxation Dispersionmentioning

confidence: 99%

Water molecule binding and lifetimes on the DNA duplex d(CGCGAATTCGCG)2

Zhou

Bryant

1996

J Biomol NMR

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Measurements of the water proton spin-lattice relaxation rate for aqueous solutions of the palindromic dodecamer, d(CGCGAATTCGCG)2, are reported as a function of the magnetic field strength. The magnitude of the relaxation rates at low magnetic field strengths and the shape of the relaxation dispersion curve permit assessment of the number of water molecules which may be considered bound to the DNA for a time equal to or longer than the rotational correlation time of the duplex. The data are examined using limiting models that arbitrarily use the measured rotational correlation time of the polynucleotide complex as a reference point for the water molecule lifetime. If it is assumed that water molecules are bound at DNA sites for times as long as or longer than the rotational correlation time of the duplex, then the magnitude of the relaxation rates at low field require that there may be only two or three such water sites. However, if the lifetime constraint is relaxed, and we assume that the number of water molecules bound to the DNA is more nearly the number identified in the X-ray structures, then the average water molecule lifetime is on the order of 1 ns. Measurements of 1H NOESY spectra demonstrate that some water molecules must have lifetimes sufficiently long that negative Overhauser effects are observed. Taken together, these results suggest a distribution of water molecule lifetimes in which most of the DNA-bound water molecule lifetimes are shorter than the rotational correlation time of the duplex, but where some have lifetimes of at least 1 ns under these concentrated conditions.

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Magnetization transfer, cross‐relaxation, and chemical exchange in rotationally immobilized protein gels

Cited by 31 publications

References 35 publications

On the Importance of Exchangeable NH Protons in Creatine for the Magnetic Coupling of Creatine Methyl Protons in Skeletal Muscle

On the Importance of Exchangeable NH Protons in Creatine for the Magnetic Coupling of Creatine Methyl Protons in Skeletal Muscle

Temperature dependence and phase transition of proton relaxation of hydrated collagen in intact beef tendon specimens via cross‐relaxation spectroscopy

Water molecule binding and lifetimes on the DNA duplex d(CGCGAATTCGCG)2

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