Protein conformational changes induced by guanidine at predenaturational concentrations.

Abstract

The nature of the molecular event that apomyoglobin undergoes at predenaturational concentrations of guanidine has been investigated by means of steady-state and multifrequency phase and modulation fluorometry. The results have been compared to those observed for liver alcohol dehydrogenase. From these studies has been hypothesized a different susceptibility of the distinct elements of secondary, super-secondary, and tertiary structure towards the denaturing action of guanidine at predenaturational concentrations.

Cite this paper

@article{Bismuto1988ProteinCC, title={Protein conformational changes induced by guanidine at predenaturational concentrations.}, author={Ettore Bismuto and Gaetano Irace}, journal={International journal of peptide and protein research}, year={1988}, volume={32 5}, pages={321-5} }