Heterogeneous folding landscapes and predetermined breaking points within a protein family.

ABSTRACT: The accurate prediction of protein structures with artificial intelligence has been a spectacular success. Yet, how proteins fold into their native structures inside the cell remains incompletely understood. Of particular interest is to rationalize how proteins interact with the protein homeostasis network, an organism specific set of protein folding and quality control enzymes. Failure of protein homeostasis leads to widespread misfolding and aggregation, and thus neurodegeneration. Here, I present a comparative analysis of the folding of 16 single-domain proteins from the same organism across a protein family, the Saccharomyces cerevisiae small GTPases. Using computational modeling to directly probe protein folding dynamics, this work shows how near identical structures from the same fol

SUBMITTER: Pechmann S 

PROVIDER: S-EPMC11571096 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature