Stengle, Thomas R. and Baldeschwieler, John D. (1966) Halide ions as chemical probes for NMR studies of proteins. Proceedings of the National Academy of Sciences of the United States of America, 55 (5). pp. 1020-1025. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:STEpnas66
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There has been considerable recent interest in the application of nuclear magnetic resonance techniques to the study of biological macromolecules.(1) NMR is in general not sufficiently sensitive for the direct study of biomolecules in solution at realistic concentrations. Some of the most promising developments have therefore involved the use of nuclear relaxation effects to probe gross molecular structural features.(2) These techniques frequently rely on the effects of small concentrations of paramagnetic atoms on the relaxation times of solvent nuclei,(3-5) or on the binding and exchange of small molecules with proteins.(6) Although paramagnetic relaxation effects have been widely exploited to yield structural information on relatively simple inorganic complexes in solution,(7-9) these techniques usually suffer from the inherent complexity of the relaxation process.(2) The observed effects on nuclear relaxation are usually the result of several competing mechanisms of comparable significance, which makes interpretation of line shapes in terms of molecular events hazardous.
|Additional Information:||Copyright © 1966 by the National Academy of Sciences. Communicated by Harden M. McConnell, March 9, 1966. Helpful discussions with Professors H. M. McConnell, H. Taube, and L. Stryer are gratefully acknowledged. This research was supported by the National Science Foundation under grant GP4924, and by the National Institutes of Health under grant GM-13545-01. One of us (Thomas R. Stengle) was also supported in part by the Center for Materials Research, Stanford University.|
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|Deposited By:||Tony Diaz|
|Deposited On:||06 Jan 2006|
|Last Modified:||26 Dec 2012 08:43|
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