Evidence map›Paper›PMID 35129957›Full record

ArticleACS biomaterials science & engineering2022

End-to-End Deep Learning Model to Predict and Design Secondary Structure Content of Structural Proteins.

Chi-Hua Yu, Wei Chen, Yu-Hsuan Chiang, Kai Guo, Zaira Martin Moldes, David L Kaplan, Markus J Buehler

Abstract read
In one paragraph

Article in ACS biomaterials science & engineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Protein subcellular localization prediction tools.Computational and structural biotechnology journal · 2024
    Review
  7. Article
  8. Review
  9. ProtAgents: protein discoveryDigital discovery · 2024
    Article
  10. Article
  11. Article
  12. Untapped Potential of Deep Eutectic Solvents for the Synthesis of Bioinspired Inorganic-Organic Materials.Chemistry of materials : a publication of the American Chemical Society · 2023
    Review
  13. Review
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Chi-Hua YuLaboratory for Atomistic and Molecular Mechanics (LAMM), Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.
Wei ChenDepartment of Engineering Science, National Cheng Kung University, No.1, University Road, Tainan City 701, Taiwan.
Yu-Hsuan ChiangDepartment of Civil Engineering, National Cheng Kung University, No.1, University Road, Tainan City 701, Taiwan.
Kai GuoLaboratory for Atomistic and Molecular Mechanics (LAMM), Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.ORCID 0000-0003-2557-0061
Zaira Martin MoldesDepartment of Biomedical Engineering, Tufts University, Medford, Massachusetts 02155, United States.ORCID 0000-0002-2932-8064
David L KaplanDepartment of Biomedical Engineering, Tufts University, Medford, Massachusetts 02155, United States.ORCID 0000-0002-9245-7774
Markus J BuehlerLaboratory for Atomistic and Molecular Mechanics (LAMM), Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States.ORCID 0000-0002-4173-9659

Funding

Models to Predict Protein Biomaterial PerformanceU01EB014976 · NIBIB · TUFTS UNIVERSITY MEDFORD · PI BUEHLER, MARKUS J., KAPLAN, DAVID L. · 2012 to 2020
$5.2M
NIBIB NIH HHS U01 EB014976
6 · The paper itself

Abstract

Structural proteins are the basis of many biomaterials and key construction and functional components of all life. Further, it is well-known that the diversity of proteins' function relies on their local structures derived from their primary amino acid sequences. Here, we report a deep learning model to predict the secondary structure content of proteins directly from primary sequences, with high computational efficiency. Understanding the secondary structure content of proteins is crucial to designing proteins with targeted material functions, especially mechanical properties. Using convolutional and recurrent architectures and natural language models, our deep learning model predicts the content of two essential types of secondary structures, the α-helix and the β-sheet. The training data are collected from the Protein Data Bank and contain many existing protein geometries. We find that our model can learn the hidden features as patterns of input sequences that can then be directly related to secondary structure content. The α-helix and β-sheet content predictions show excellent agreement with training data and newly deposited protein structures that were recently identified and that were not included in the original training set. We further demonstrate the features of the model by a search for de novo protein sequences that optimize max/min α-helix/β-sheet content and compare the predictions with folded models of these sequences based on

Indexed as

Deep LearningAmino Acid SequenceProteinsProtein Structure, SecondaryProteinsartificial intelligencedeep learningmateriomicsprotein structuresecondary structurestructural proteins

Identifiers

PMID35129957
PMCPMC9347213

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.