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This is a Experimental Study study.

October 11, 2025

Cooperative Metastability Preserves Native-like Protein Structures in the Gas Phase

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Myoglobin retains a native-like structure in the absence of solvent, and cooperative metastability plays a crucial role.
Experimental and computed ion mobility spectra validate the integrated approach across charge states and activation regimes.
Proteins undergo two distinct unfolding steps, maintaining compactness through non-local salt bridges before expanding.
The findings emphasize that solvent-free proteins with weakly coupled components may unfold independently.

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Experimental findings show cooperative metastability preserves myoglobin structure in gas phase, indicating key interactions persist.

Bleiholder et al. (2025) studied this question.

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