Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation.

ABSTRACT: The aggregation of proteins compromises cell fitness, either because it titrates functional proteins into non-productive inclusions or because it results in the formation of toxic assemblies. Accordingly, computational proteome-wide analyses suggest that prevention of aggregation upon misfolding plays a key role in sequence evolution. Most proteins spend their lifetimes in a folded state; therefore, it is conceivable that, in addition to sequences, protein structures would have also evolved to minimize the risk of aggregation in their natural environments. By exploiting the AGGRESCAN3D structure-based approach to predict the aggregation propensity of >600 Escherichia coli proteins, we show that the structural aggregation propensity of globular proteins is connected with their abundance, le

SUBMITTER: Carija A 

PROVIDER: S-EPMC6721704 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature