ArticleACS omega2026
Examining Protein Residue-Level Stability Using Theory and Experiment.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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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.
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.
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Who cites it
0 citing papers in PubMed.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein behavior, whether evolved in nature or intentionally designed, is governed by the energetics of amino acid interactions that bridge sequence to function. As an extension of the theory of protein folding funnels, local frustration quantifies the optimality of these residue-level interactions relative to alternatives. Although this framework has existed for decades, experimental validation has remained elusive. Past deep mutational scanning datasets enable experimental assessment across nearly 8,000 positions from 178 proteins. Results provide experimental evidence for theoretical predictions regarding the relationship between local frustration and protein sequence, structure, and evolution. An evaluation of three
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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.