Feb 1, 1973

Solvent proton magnetic relaxation dispersion in solutions of concanavalin A

Proceedings of the National Academy of Sciences of the United States of America
S H KoenigC F Brewer


Concanavalin A, a protein isolated from jack beans, exhibits several important biological properties, all of which are related to its ability to bind and precipitate specific polysaccharides. Concanavalin A is a dimer at pH 5.6, and has one transition-metal and one calcium-ion binding site per monomer unit of molecular weight 27,000. Both metal-ion sites must be occupied for the protein to be active. It is of interest to determine the role of the transition metal ion in Concanavalin A and its relationship to the sugar binding activity of the protein. We report the magnetic field and temperature dependences of the spin-lattice magnetic relaxation rates of solvent protons in aqueous solutions of zinc and manganese derivatives of Concanavalin A, and the influence of monosaccharide binding on these rates. The results of a leastsquares fit of the data to the theory, with five adjustable parameters, indicate that there is one rapidly exchanging water molecule ligand on the Mn(2+) ion, with a residence lifetime of 2.5 musec at 25 degrees , and with its protons 0.27 nm (2.7 A) from the Mn(2+) ion. We find that at low magnetic fields (proton Larmor frequencies below about 10 MHz), the correlation time for the dipolar interaction between...Continue Reading

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Mentioned in this Paper

In Vivo NMR Spectroscopy
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Concanavalin A

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