Thermally versus Chemically Denatured Protein States.

ABSTRACT: Protein unfolding thermodynamic parameters are conventionally extracted from equilibrium thermal and chemical denaturation experiments. Despite decades of work, the degree of structure and the compactness of denatured states populated in these experiments are still open questions. Here, building on previous works, we show that thermally and chemically denatured protein states are distinct from the viewpoint of far-ultraviolet circular dichroism experiments that report on the local conformational status of peptide bonds. The differences identified are independent of protein length, structural class, or experimental conditions, highlighting the presence of two sub-ensembles within the denatured states. The sub-ensembles, U_T and U_D for thermally induced and denaturant-in

SUBMITTER: Narayan A 

PROVIDER: S-EPMC6542680 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature