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James F. Hinton CHEM 210 |
Degrees:
Ph.D., University of Georgia, 1964
Postdoctoral Research Associate; University of Georgia, 1964-65
Postdoctoral Research Associate; University of Arkansas, 1965-67
U of A Alumni Award for Research; 1981
Research Interests:
NMR spectroscopy
Research:
The research efforts of this group are involved with the development and application of NMR techniques to a variety of problems. These include the use of metal cation NMR spectroscopy to study the binding and transport of monovalent cations by molecules that reside in membranes and serve as cation transport agents, and molecular modeling of the conformation of channel forming proteins using distance constraints obtained by 2D and 3D NMR. A very active program has been developed in the study of monovalent cation transport across membranes, facilitated by carrier molecules and channel forming proteins. This investigation involves the use of TI-205, Na-23, K-39, and Xe-129 spectroscopy to determine the thermodynamics for the binding of monovalent cations to the channel formed by gramicidin-A and analogs of this protein. Using the NMR technique of magnetization inversion transfer (Figure. 1), the rate parameters for the transport process can be detained. From the determination of these parameters for a number of site directed single amino acid substituted gramicidin analogs, a quantitative structure- function relationship is being developed for this very important biological monovalent cation transport system.
This program involves extensive NMR technique development and application (1 and 2D and 3D, Figure. 2), membrane production and handling, as well as peptide synthesis and purification. 2D NMR techniques such as DQCOSY TOCSY, ROESY and NOESY are used to make proton assignments and to obtain distance constraints for gramicidin incorporated into micelles and vesicles. The distance constraints are then used in molecular dynamics procedures to determine a 3D structure of the gramicidin channel. These techniques are also being applied to the study of the acetylcholine receptor channel.
In collaboration with Professor Pulay, programs and hardware are being developed for the calculation of NMR chemical shifts using ab initio quantum mechanical techniques.