ArticleProtein science : a publication of the Protein Society2024
High-throughput system for the thermostability analysis of proteins.
Article in Protein science : a publication of the Protein Society, 2024. 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.
- MAXTIA: A high-throughput platform for rapid functional epitope mapping by kinetic screening of mutant libraries.Protein science : a publication of the Protein Society · 2026Article
- Thermostability Engineering in Therapeutic Antioxidant Enzymes: From Molecular Fundamentals to Oxidative Stress Applications.International journal of molecular sciences · 2026Review
- Directed evolution of enzymes at the crossroads of tradition and innovation.FEBS open bio · 2026Review
- Aptamers and aptamer-drug conjugates as synthetic immune modulators for cancer immunotherapy.Frontiers in immunology · 2026Review
- Accelerating antibody discovery and optimization with high-throughput experimentation and machine learning.Journal of biomedical science · 2025Review
- High-throughput system for the thermostability analysis of proteins.Protein science : a publication of the Protein Society · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Thermal stability of proteins is a primary metric for evaluating their physical properties. Although researchers attempted to predict it using machine learning frameworks, their performance has been dependent on the quality and quantity of published data. This is due to the technical limitation that thermodynamic characterization of protein denaturation by fluorescence or calorimetry in a high-throughput manner has been challenging. Obtaining a melting curve that derives solely from the target protein requires laborious purification, making it far from practical to prepare a hundred or more samples in a single workflow. Here, we aimed to overcome this throughput limitation by leveraging the high protein secretion efficacy of Brevibacillus and consecutive treatment with plate-scale purification methodologies. By handling the entire process of expression, purification, and analysis on a per-plate basis, we enabled the direct observation of protein denaturation in 384 samples within 4 days. To demonstrate a practical application of the system, we conducted a comprehensive analysis of 186 single mutants of a single-chain variable fragment of nivolumab, harvesting the melting temperature (T
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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.