Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed βα protein.

ABSTRACT: The successful de novo design of proteins can provide insights into the physical chemical basis of stability, the role of evolution in constraining amino acid sequences, and the production of customizable platforms for engineering applications. Previous guanidine hydrochloride (GdnHCl; an ionic denaturant) experiments of a designed, naturally occurring βα fold, Di-III_14, revealed a cooperative, two-state unfolding transition and a modest stability. Continuous-flow mixing experiments in our laboratory revealed a simple two-state reaction in the microsecond to millisecond time range and consistent with the thermodynamic results. In striking contrast, the protein remains folded up to 9.25 M in urea, a neutral denaturant, and hydrogen exchange (HDX) NMR analysis in water revealed the presence

SUBMITTER: Basak S 

PROVIDER: S-EPMC6452746 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature