
doi: 10.1002/prot.21969
pmid: 18260111
AbstractThe aggregation of Zn(II)‐bound and zinc‐free human insulin was studied in solution using the Hβ∼CH3 crosspeaks of threonine residues in 2D COSY, TOCSY, and NOESY NMR spectra which allow viewing of the oligomers in equilibrium. This is complemented by PFGSE measurements of the translational diffusion coefficient, Di, used for monitoring the changes in equilibrium composition of aggregates on dilution of both insulins in physiological medium. The back calculation of the dilution isotherm allows establishing the association constants for oligomeric equilibria in solution and discussion of the models of association. Proteins 2008. © 2008 Wiley‐Liss, Inc.
Zinc, Models, Chemical, Humans, Insulin, Nuclear Magnetic Resonance, Biomolecular, Electrophoresis, Gel, Pulsed-Field, Protein Binding
Zinc, Models, Chemical, Humans, Insulin, Nuclear Magnetic Resonance, Biomolecular, Electrophoresis, Gel, Pulsed-Field, Protein Binding
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