Limits and potential of combined folding and docking.

ABSTRACT:

Motivation

In the last decade, de novo protein structure prediction accuracy for individual proteins has improved significantly by utilising deep learning (DL) methods for harvesting the co-evolution information from large multiple sequence alignments (MSAs). The same approach can, in principle, also be used to extract information about evolutionary-based contacts across protein-protein interfaces. However, most earlier studies have not used the latest DL methods for inter-chain contact distance prediction. This article introduces a fold-and-dock method based on predicted residue-residue distances with trRosetta.

Results

The method can simultaneously predict the tertiary and quaternary structure of a protein pair, even when the structures of the monomers are not known. The s

SUBMITTER: Pozzati G 

PROVIDER: S-EPMC8796369 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature