The research proposed in this competitive renewal application will continue theoretical and experimental investigations of magnetic relaxation coupling, a crucial component of proton spin relaxation in tissue and other dynamically inhomogeneous systems of biological interest. Such coupling may be exploited to provide an additional mechanism for achieving altered magnetic resonance image contrast thereby permitting superimposition of structural and/or dynamic information about the solid components on the magnetic resonance behavior of the solvent water. Such protocols for the enhancement of image contrast are becoming increasingly useful in clinical radiology. Previous work, some of which is quite imaginative and novel, from the principal investigator's laboratory has provided a secure foundation for the proposed studies which depend in part on a mechanistic understanding of proton cross relaxation. Such insight has largely been obtained for purified protein systems in solution and gel states which have been appropriately modified to mimic magnetic relaxation occurring in tissue. Studies are proposed which fall into the following categories: (1) definition of the mechanisms important for magnetization transfer in tissue component systems more complex than isolated protein gels and protein solutions; (2) definition of water molecule and other solvent molecule binding site structures and measure solvent molecule lifetimes for buried solvent molecules; (3) measurement of the changes in amide hydrogen exchange rates in low molecular weight proteins in response to hydrostatic pressure and time dependent electromagnetic fields; (4) characterization of the relaxation and dynamics of molecules in restricted high surface area geometrically constrained environments.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM034541-13
Application #
2459366
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1984-07-01
Project End
2000-07-31
Budget Start
1997-08-01
Budget End
1998-07-31
Support Year
13
Fiscal Year
1997
Total Cost
Indirect Cost
Name
University of Virginia
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
001910777
City
Charlottesville
State
VA
Country
United States
Zip Code
22904
Teng, Ching-Ling; Hinderliter, Brian; Bryant, Robert G (2006) Oxygen accessibility to ribonuclease a: quantitative interpretation of nuclear spin relaxation induced by a freely diffusing paramagnet. J Phys Chem A 110:580-8
Teng, Ching-Ling; Bryant, Robert G (2004) Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopy. Biophys J 86:1713-25
Teng, Ching-Ling; Martini, Silvia; Bryant, Robert G (2004) Local measures of intermolecular free energies in solution. J Am Chem Soc 126:15253-7
Victor, Ken G; Teng, Ching-Ling; Dinesen, T R D et al. (2004) Magnetic relaxation dispersion of lithium ion in solutions of DNA. Magn Reson Chem 42:518-23
Korb, Jean-Pierre; Bryant, Robert G (2002) Magnetic field dependence of proton spin-lattice relaxation times. Magn Reson Med 48:21-6
Teng, C L; Hong, H; Kiihne, S et al. (2001) Molecular oxygen spin-lattice relaxation in solutions measured by proton magnetic relaxation dispersion. J Magn Reson 148:31-4
Zhang, H; Lizitsa, N; Bryant, R G et al. (2001) Experimental characterization of intermolecular multiple-quantum coherence pumping efficiency in solution NMR. J Magn Reson 148:200-8
Dixon, M E; Hitchens, T K; Bryant, R G (2000) Comparisons of pressure and temperature activation parameters for amide hydrogen exchange in T4 lysozyme. Biochemistry 39:248-54
Kiihne, S; Bryant, R G (2000) Protein-bound water molecule counting by resolution of (1)H spin-lattice relaxation mechanisms. Biophys J 78:2163-9
Danek, A N; Bryant, R G (2000) Decay of dipolar order in diamagnetic and paramagnetic proteins and protein gels. J Magn Reson 143:35-8

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