PROLINE ISOMERIZATION IN UNFOLDED RIBONUCLEASE-A - THE EQUILIBRIUM BETWEEN FAST-FOLDING AND SLOW-FOLDING SPECIES IS INDEPENDENT OF TEMPERATURE
- 1 January 1982
- journal article
- research article
- Vol. 128 (1) , 77-80
Abstract
Unfolded [bovine pancreas] RNase A consists of a mixture of fast refolding (UF) and slow-refolding (US) species. The slow UF .dblarw. US equilibration reaction is rate-limited by proline peptide bond isomerization. Investigations of the dependence on temperature of the UF .dblarw. US equilibrium have led to conflicting results and different molecular interpretations. Here the dependence on temperature of the UF:US ratio was reinvestigated by using a new assay for the fast-folding molecules UF. Between 0.degree. C and 60.degree. C the proportion of UF present in unfolded RNase A at 6 M guanidine.cntdot.HCl was independent of temperature. Consequently, no conclusions can be drawn regarding the role and importance of particular prolines in the UF .dblarw. US transition solely from these results.This publication has 19 references indexed in Scilit:
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