The effects of salts on the stability of the collagen helix under acidic conditions.

Abstract

In the acid pH region, the relative effects of various salts on the thermal stability of the collagen helix are quite different from their effects at neutral pH. The magnitude of the decrease in thermal stability brought about by the salts studied depends mainly on the nature and concentration of the anion and very little on the nature of the cation, whereas at neutral pH the nature of both anions and cations affects the collagen helix stability, the effects of the two ions being roughly additive. The magnitude of the effect of salts at acid pH is much greater than that at neutral pH whereas for a non-ionized denaturant, urea, the magnitudes at both neutral and acid pH are similar. The data are discussed in terms of possible interactions between salts and the positively charged protein with particular consideration of the effects of salts on the pKa of protein carboxyl groups.