Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Single-sequence protein structure prediction using supervised transformer protein language models

Wenkai Wang, Zhenling Peng, View ORCID ProfileJianyi Yang
doi: https://doi.org/10.1101/2022.01.15.476476
Wenkai Wang
1School of Mathematical Sciences, Nankai University, Tianjin 300071, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Zhenling Peng
2Research Center for Mathematics and Interdisciplinary Sciences, Shandong University, Qingdao, 266237, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Jianyi Yang
1School of Mathematical Sciences, Nankai University, Tianjin 300071, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Jianyi Yang
  • For correspondence: yangjy@nankai.edu.cn
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Supplementary material
  • Preview PDF
Loading

Abstract

It remains challenging for single-sequence protein structure prediction with AlphaFold2 and other deep learning methods. In this work, we introduce trRosettaX-Single, a novel algorithm for singlesequence protein structure prediction. It is built on sequence embedding from s-ESM-1b, a supervised transformer protein language model optimized from the pre-trained model ESM-1b. The sequence embedding is fed into a multi-scale network with knowledge distillation to predict inter-residue 2D geometry, including distance and orientations. The predicted 2D geometry is then used to reconstruct 3D structure models based on energy minimization. Benchmark tests show that trRosettaX-Single outperforms AlphaFold2 and RoseTTAFold on natural proteins. For instance, with single-sequence input, trRosettaX-Single generates structure models with an average TM-score ~0.5 on 77 CASP14 domains, significantly higher than AlphaFold2 (0.35) and RoseTTAFold (0.34). Further test on 101 human-designed proteins indicates that trRosettaX-Single works very well, with accuracy (average TM-score 0.77) approaching AlphaFold2 and higher than RoseTTAFold, but using much less computing resource. On 2000 designed proteins from network hallucination, trRosettaX-Single generates structure models highly consistent to the hallucinated ones. These data suggest that trRosettaX-Single may find immediate applications in de novo protein design and related studies. trRosettaX-Single is available through the trRosetta server at: http://yanglab.nankai.edu.cn/trRosetta/.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
Back to top
PreviousNext
Posted January 18, 2022.
Download PDF

Supplementary Material

Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Single-sequence protein structure prediction using supervised transformer protein language models
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Single-sequence protein structure prediction using supervised transformer protein language models
Wenkai Wang, Zhenling Peng, Jianyi Yang
bioRxiv 2022.01.15.476476; doi: https://doi.org/10.1101/2022.01.15.476476
Digg logo Reddit logo Twitter logo Facebook logo Google logo LinkedIn logo Mendeley logo
Citation Tools
Single-sequence protein structure prediction using supervised transformer protein language models
Wenkai Wang, Zhenling Peng, Jianyi Yang
bioRxiv 2022.01.15.476476; doi: https://doi.org/10.1101/2022.01.15.476476

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Bioinformatics
Subject Areas
All Articles
  • Animal Behavior and Cognition (3497)
  • Biochemistry (7341)
  • Bioengineering (5317)
  • Bioinformatics (20248)
  • Biophysics (9999)
  • Cancer Biology (7734)
  • Cell Biology (11291)
  • Clinical Trials (138)
  • Developmental Biology (6431)
  • Ecology (9943)
  • Epidemiology (2065)
  • Evolutionary Biology (13311)
  • Genetics (9358)
  • Genomics (12575)
  • Immunology (7696)
  • Microbiology (18998)
  • Molecular Biology (7432)
  • Neuroscience (40971)
  • Paleontology (300)
  • Pathology (1228)
  • Pharmacology and Toxicology (2133)
  • Physiology (3154)
  • Plant Biology (6855)
  • Scientific Communication and Education (1272)
  • Synthetic Biology (1895)
  • Systems Biology (5309)
  • Zoology (1087)