ArticleNature chemistry2026
Computational design of superstable proteins through maximized hydrogen bonding.
Article in Nature chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Global analysis of thermal and chemical denaturation using CheMelt: Thermodynamic dissection of highly thermostable de novo designed proteins.Protein science : a publication of the Protein Society · 2026Article
- Assembly delivery of bioactive matters: Advances, challenges, and prospects.Journal of advanced research · 2026Review
- Artificial intelligence virtual bone organoids (AIVBOs).Journal of orthopaedic translation · 2026Review
- Advances in Carrageenases: Molecular Engineering, Immobilization Techniques, and Biomedical Potential of Carrageenan Oligosaccharides.Marine drugs · 2026Review
- Exploration Editors' Favorite Research in 2025.Exploration (Beijing, China) · 2026Article
- The cutting-edge advancements in biomaterials under the guidance of intelligence and bionics.Regenerative biomaterials · 2026Review
Corrections and comments
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Authors and funding
21 authors.
Funding
Abstract
Hydrogen bonds are fundamental chemical interactions that stabilize protein structures, particularly in β sheets, enabling resistance to mechanical stress and environmental extremes. Here, inspired by natural mechanostable proteins with shearing hydrogen bonds, such as titin and silk fibroin, we de novo designed superstable proteins by maximizing hydrogen-bond networks within force-bearing β strands. Using a computational framework combining artificial intelligence-guided structure and sequence design with all-atom molecular dynamics MD simulations, we systematically expanded protein architecture, increasing the number of backbone hydrogen bonds from 4 to 33. The resulting proteins exhibited unfolding forces exceeding 1,000 pN, about 400% stronger than the natural titin immunoglobulin domain, and retained structural integrity after exposure to 150 °C. This molecular-level stability translated directly to macroscopic properties, as demonstrated by the formation of thermally stable hydrogels. Our work introduces a scalable and efficient computational strategy for engineering robust proteins, offering a generalizable approach for the rational design of resilient protein systems for extreme environments.
Indexed as
Identifiers
41254310What OpenQuestion holds
Registered trials
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.