Nuclear magnetic resonance relaxation in aqueous bovine albumin solutions

Abstract

Water proton relaxation times have been measured in aqueous solutions of bovine plasma albumin and chemically modified forms of bovine serum albumin to which NaH₂PO₄, NaCl, LiBr and LiCl were added. The observed changes in T₁ produced by denaturing the protein are consisent with a spin diffusion contribution to the relaxation rate being present in solutions of native protein. The T₂ results can be understood in terms of an exchange of protons between protein and water.