Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.

ABSTRACT: Sequence-encoded folding is the foundation of protein structure and is also possible in synthetic chains of artificial chemical composition. In natural proteins, the characteristics of the unfolded state are as important as those of the folded state in determining folding energetics. While much is known about folded structures adopted by artificial protein-like chains, corresponding information about the unfolded states of these molecules is lacking. Here, we report the consequences of altered backbone composition on the structure, stability, and dynamics of the folded and unfolded states of a compact helix-rich protein. Characterization through a combination of biophysical experiments and atomistic simulation reveals effects of backbone modification that depend on both the type of artific

SUBMITTER: Santhouse JR 

PROVIDER: S-EPMC9580521 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature