Abstract
A variety of functionally important protein properties, such as
secondary structure, transmembrane topology and solvent accessibility,
can be encoded as a labeling of amino acids. Indeed, the prediction of
such properties from the primary amino acid sequence is one of the core
projects of computational biology. Accordingly, a panoply of approaches
have been developed for predicting such properties; however, most such
approaches focus on solving a single task at a time. Motivated by
recent, successful work in natural language processing, we propose to
use multitask learning to train a single, joint model that
exploits the dependencies among these various labeling tasks. We
describe a deep neural network architecture that, given a protein
sequence, outputs a host of predicted local properties, including
secondary structure, solvent accessibility, transmembrane topology,
signal peptides and DNA-binding residues. The network is trained jointly
on all these tasks in a supervised fashion, augmented with a novel form
of semi-supervised learning in which the model is trained to
distinguish between local patterns from natural and synthetic protein
sequences. The task-independent architecture of the network obviates the
need for task-specific feature engineering. We demonstrate that, for
all of the tasks that we considered, our approach leads to statistically
significant improvements in performance, relative to a single task
neural network approach, and that the resulting model achieves
state-of-the-art performance.
| Original language | English |
|---|---|
| Article number | e32235 |
| Number of pages | 11 |
| Journal | PLoS ONE |
| Volume | 7 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2012 |
| MoE publication type | A1 Journal article-refereed |
Funding
This work was funded by NIH awards R01 GM074257 and P41 RR0011823, and by the Academy of Finland and the Finnish Cultural Foundation.
Fingerprint
Dive into the research topics of 'A unified multitask architecture for predicting local protein properties'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver