Robust folding of a de novo designed ideal protein even with most of the core mutated to valine.

ABSTRACT: Protein design provides a stringent test for our understanding of protein folding. We previously described principles for designing ideal protein structures stabilized by consistent local and nonlocal interactions, based on a set of rules relating local backbone structures to tertiary packing motifs. The principles have made possible the design of protein structures having various topologies with high thermal stability. Whereas nonlocal interactions such as tight hydrophobic core packing have traditionally been considered to be crucial for protein folding and stability, the rules proposed by our previous studies suggest the importance of local backbone structures to protein folding. In this study, we investigated the robustness of folding of de novo designed proteins to the reduction of th

SUBMITTER: Koga R 

PROVIDER: S-EPMC7739874 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature