The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure.

ABSTRACT: Interest in the structural and dynamic properties of unfolded proteins has increased in recent years owing to continued interest in protein folding and misfolding. Knowledge of the unfolded state under native conditions is particularly important for obtaining a complete picture of the protein folding process. The C-terminal domain of protein L9 is a globular alpha, beta protein with an unusual mixed parallel and antiparallel beta-strand structure. The folding kinetics and equilibrium unfolding of CTL9 strongly depend on pH, and follow a simple two state model. Both the native and the unfolded state can be significantly populated at pH 3.8 in the absence of denaturant, allowing the native state and the unfolded state to be characterized under identical conditions. Backbone (15)N, (13)C, (1)

SUBMITTER: Shan B 

PROVIDER: S-EPMC3319011 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature