Author

K. Ohshimo

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#protein folding Oct 2026

Cytochrome c is Highly Compact upon Transfer into the Gas Phase from Strong Acids as Revealed by High-Pressure ESI Ion Mobility-Mass Spectrometry

A substantial increase in the acidity of the protein solution (e.g., from pH 2 to pH 1) is known to induce the compaction of fully unfolded proteins, such as cytochrome c, into a non-native yet highly compact molten globule state, referred to as the A-state. In this study, the conformational landscape of the gaseous...

Shunsuke Kamioka, K. Ohshimo, D. Asakawa et al. · Journal of the American Soci... · 0 citations

Open access Aug 2026

K+-Selective Compaction of Flexible Ionophore PF1022A: Conformational Landscapes of Alkali Metal Complexes.

The natural cyclic octadepsipeptide ionophore PF1022A (PFA) selectively transports physiologically relevant K+ over Na+ across lipid membranes; however, its underlying structural mechanism remains unclear. Here, variable-temperature ion mobility mass spectrometry and theoretical calculations revealed the conformational...

Shunsuke Kamioka, Ryosuke Ito, K. Ohshimo et al. · Journal of Physical Chemistr... · 0 citations

Aug 2026

Elucidating Protomer Structures and Fragmentation Dynamics of Protonated Aminobenzoic and Aminocinnamic Acids via Cryo-Ion Mobility and Laser Spectroscopy.

Biological and synthetic systems featuring coexisting amino and carboxy groups, such as amino acids and peptides, serve as vital models for understanding hydrogen-bonded proton transport networks. Unambiguously identifying protonation isomers (protomers) is crucial yet challenging, as their structures are heavily modul...

Y. Inokuchi, Kengo Tsunoda, Amiru Ohata et al. · Journal of Physical Chemistr... · 0 citations