Osmolyte Structural and Thermodynamic Effects Across the Protein Folding Landscape.

ABSTRACT: In this work, the structure and thermodynamics of urea and trimethylamine N-oxide (TMAO) preferential interactions across the complete folding landscape of the β-sheet SRC Homology 3 (SH3) domain and the helical B domain of protein A (BdpA) are characterized. There is a high correlation between preferential interactions and the surface area of the denatured states, despite the chemical nature of the exposed surfaces upon denaturation differing from those of native states. For SH3, the denaturation always proceeds with an increase in surface area, such that the qualitative effect of cosolvents on the stability of all denatured states can be inferred from the preferential interactions in the native state. On the other hand, for BdpA, partially denatured states exist that are destabilized by

SUBMITTER: Pereira AF 

PROVIDER: S-EPMC12728603 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature