ArticleMethods in molecular biology (Clifton, N.J.)2026
Mitochondrial Transmembrane β-Barrels: Deducing Thermodynamic Regulators of Folding and Stability.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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.
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Authors and funding
3 authors.
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Abstract
Biophysical characterization of membrane protein folding and stability provides a direct molecular correlation of folding and stability with protein function. Here, we describe how mitochondrial outer membrane β-barrels can be overproduced, and how structures of folding intermediates and per-residue thermodynamic stability are measured using intrinsic tryptophan fluorescence in near-native membranes.
Indexed as
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42156699What 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.