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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.

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Mitochondrial Transmembrane β-Barrels: Deducing Thermodynamic Regulators of Folding and Stability

  • 实验方案

  • 发表日期：

    2026年

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  • Udit Kumar Dash,
  • Kinjal Mazumder,
  • Radhakrishnan Mahalakshmi

摘要

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.