What question did this study set out to answer?

This research aims to elucidate which structural features of holo-myoglobin remain in the absence of solvent and how denaturation occurs in vacuo.

March 29, 2026JACS AuOpen Access

Native-Like Protein Structures in Vacuo: Steric Cooperativity as a Kinetic Barrier to Denaturation

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Investigation of gas-phase denaturation in holo-myoglobin reveals steric cooperativity as a crucial kinetic barrier.

This research aims to elucidate which structural features of holo-myoglobin remain in the absence of solvent and how denaturation occurs in vacuo.
Utilized native mass spectrometry to analyze protein structures in gas-phase.
Applied tandem-trapped ion mobility spectrometry and tandem-mass spectrometry (Tandem-TIMS) for detailed investigation.
Employed molecular dynamics simulations to understand denaturation pathways.
Holo-myoglobin retains its α-helical fold and core architecture in the gas phase.
Denaturation displays a hierarchical mechanism, starting from compact shapes to global unfolding.
Denaturation is largely insensitive to salt-bridge rearrangements, indicating steric constraints are significant.

Bleiholder et al. (2026) studied this question.

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