A Method for Assessing the Robustness of Protein Structures by Randomizing Packing Interactions.

ABSTRACT: Many single-domain proteins are not only stable and water-soluble, but they also populate few to no intermediates during folding. This reduces interactions between partially folded proteins, misfolding, and aggregation, and makes the proteins tractable in biotechnological applications. Natural proteins fold thus, not necessarily only because their structures are well-suited for folding, but because their sequences optimize packing and fit their structures well. In contrast, folding experiments on the de novo designed Top7 suggest that it populates several intermediates. Additionally, in de novo protein design, where sequences are designed for natural and new non-natural structures, tens of sequences still need to be tested before success is achieved. Both these issues may be

SUBMITTER: Yadahalli S 

PROVIDER: S-EPMC9271847 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature