A detailed understanding of the structural propensities and energetics of the denatured state ensemble is a critical piece of the folding puzzle. Unfolded states are the starting point for protein folding, aggregation and amyloid formation. The presence of long-range interactions in the DSE may limit the conformational search early in the folding process and might protect aggregation prone sequences. Mutations that modulate the properties of the DSE can significantly affect protein stability, alter the tendency to aggregate and impact the analysis of folding dynamics, for example by complicating the popular phi-value approach used to characterize folding transition states.  In certain cases, the DSE can even be a target for rational protein design . We describe recent progress in characterizing the denatured state under both native and strongly denaturing conditions. In both cases the denatured state differs significantly form classic random coil models.

Role of the unfolded state in protein folding

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.