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Protein Science, Vol 1, Issue 2 236-244, Copyright © 1992 by Cold Spring Harbor Laboratory Press

ARTICLE

Equilibrium denaturation studies of mouse {beta}-nerve growth factor

D. E. TIMM and K. E. NEET
Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106

Equilibrium denaturation of dimeric mouse {beta}-nerve growth factor ({beta}-NGF) has been studied by monitoring changes in the protein's spectroscopic characteristics. Denaturation of {beta}-NGF in guanidine hydrochloride and urea resulted in an altered intrinsic fluorescence emission spectrum, fluorescence depolarization, and diminished negative circular dichroism. Native-like spectroscopic properties and specific biological activity are restored when denaturant is diluted from unfolded samples, demonstrating that this process is fully reversible. However, refolding of denatured {beta}-NGF is dependent on the three disulfide bonds present in the native protein and does not readily occur when the disulfide bonds are reduced. Graphical analysis and nonlinear least-squares fitting of {beta}-NGF denaturation data demonstrate that denaturation is dependent on the concentration of {beta}-NGF and is consistent with a two-state model involving native dimer and denatured monomer (N(2) = 2D). The conformational stability of mouse {beta}-NGF calculated according to this model is 19.3 +/- 1.1 kcal/mol in 100 mM sodium phosphate at pH 7. Increasing the hydrogen ion concentration resulted in a 25% decrease in {beta}-NGF stability at pH 4 relative to pH 7.
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