From Protein Design to the Energy Landscape of a Cold Unfolding Protein.

ABSTRACT: Understanding protein folding is crucial for protein sciences. The conformational spaces and energy landscapes of cold (unfolded) protein states, as well as the associated transitions, are hardly explored. Furthermore, it is not known how structure relates to the cooperativity of cold transitions, if cold and heat unfolded states are thermodynamically similar, and if cold states play important roles for protein function. We created the cold unfolding 4-helix bundle DCUB1 with a de novo designed bipartite hydrophilic/hydrophobic core featuring a hydrogen bond network which extends across the bundle in order to study the relative importance of hydrophobic versus hydrophilic protein-water interactions for cold unfolding. Structural and thermodynamic characterization resulted in the discovery

SUBMITTER: Pulavarti SVSRK 

PROVIDER: S-EPMC9281400 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature