Probing the Stability of a ß-Hairpin Scaffold after Desolvation.
J Phys Chem Lett
; 15(19): 5041-5046, 2024 May 16.
Article
em En
| MEDLINE
| ID: mdl-38700091
ABSTRACT
Probing the structural characteristics of biomolecular ions in the gas phase following native mass spectrometry (nMS) is of great interest, because noncovalent interactions, and thus native fold features, are believed to be largely retained upon desolvation. However, the conformation usually depends heavily on the charge state of the species investigated. In this study, we combine transition metal ion Förster resonance energy transfer (tmFRET) and ion mobility-mass spectrometry (IM-MS) with molecular dynamics (MD) simulations to interrogate the ß-hairpin structure of GB1p in vacuo. Fluorescence lifetime values and collisional cross sections suggest an unfolding of the ß-hairpin motif for higher charge states. MD simulations are consistent with experimental constraints, yet intriguingly provide an alternative structural interpretation:
preservation of the ß-hairpin is not only predicted for 2+ but also for 4+ charged species, which is unexpected given the substantial Coulomb repulsion for small secondary structure scaffolds.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transferência Ressonante de Energia de Fluorescência
/
Simulação de Dinâmica Molecular
Idioma:
En
Revista:
J Phys Chem Lett
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
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