Abstract
Measurement of nuclear magnetic relaxation rates in the presence of paramagnetic probes, an NMR method which determines distances from the individual atoms of a molecule in solution to a nearby paramagnetic reference point, has emerged in the past decade as a useful approach to the study of the conformation and arrangement of enzyme-bound substrates in solution.(1–8) Such NMR studies in solution, like X-ray diffraction in the crystalline state, detect individual atoms. The obvious advantage of observing complexes in solution, with directly measurable kinetic and thermodynamic properties, is that the relevance of such complexes to catalysis is testable.
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