Nuclear magnetic resonance determination of metal-protn distances in the EF site of carp parvalbumin using the susceptibility contribution to the line broadening of lanthanide-shifted resonances.
The substitution of the paramagnetic lanthanide ion ytterbium for the calcium ion in the EF calcium binding site of carp parvalbumin results in a series of 1H NMR resonances which are shifted well outside of the envelope of the 1H NMR spectrum of the diamagnetic form of the protein. The line broadening of these shifted resonances has been measured as a function of 1H NMR frequency between 200 and 400 MHz, and the spin-lattice relaxation rates have been measured at 270 MHz. The analysis of the relaxation rates based upon the theories of Vega & Fiat [Vega, A. J., & Fiat, D. (1976) Mol. Phys. 31, 347-355] and Guéron [Guéron, M. (1975) J. Magn. Reson. 19, 58-66] indicates that a major contribution to the line widths comes from the novel susceptibility relaxation mechanism and that the metal to proton distances can be directly calculated from this contribution.
D000818:Animals; D002347:Carps; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D008674:Metals, Rare Earth; D009124:Muscle Proteins; D010320:Parvalbumins; D011487:Protein Conformation
D008674:Metals, Rare Earth; D009124:Muscle Proteins; D010320:Parvalbumins