Energetically significant networks of coupled interactions within an unfolded protein

• DOI: 10.1073/pnas.1402054111
• Publication Date: 2014-08-07T03:11:02Z
• Authors: Jae-Hyun Cho; Wenli Meng; Satoshi Sato; Eun Young Kim; Hermann Schindelin; Daniel P. Raleigh
• Keywords: Cooperativity; Energetics; Globular protein; Folding (DSP implementation); Intrinsically Disordered Proteins; Sequence (biology)

Significance Unfolded and partially unfolded proteins participate in a wide range of biological processes from pathological aggregation to the regulation normal cellular activity. Characterization nonnative states is critical for understanding these processes, yet comparatively little known about their energetics structural propensities under native conditions. We demonstrate that energetically important interactions, which involve multiple residues include significant effects, can form denatured state ensemble (DSE) globular proteins, are distant sequence spatially well separated structure. Mutations alter DSE impact analysis cooperativity folding, could modulate propensity aggregate.