Structural Landscape of Syanodin I Lasso Peptide
∼ 865 ms) resolved at least two distinct conformers within each IMS band, revealing intramolecular interactions inaccessible by TIMS alone. QM calculations determined the HDX rate and number of accessible hydrogens for Pro10 and Gln13; this information was used to inform the MD candidate assignment of the 2D-HDX-TIMS-MS results. This workflow provides a comprehensive framework for probing biomolecular conformational dynamics through complementary solution- and gas-phase approaches. The integration of solution-phase hydrogen/deuterium exchange (HDX) with ion mobility spectrometry-mass spectrometry (IMS-MS) offers powerful structural insights into the conformational dynamics of biological molecules.
Authors
- Julian D. Hegemann (ORCID: https://orcid.org/0000-0002-3859-8744)
- Kévin Jeanne Dit Fouque (ORCID: https://orcid.org/0000-0002-2974-1350)
- Miguel Santos-Fernandez (ORCID: https://orcid.org/0000-0003-4233-0203)
- Séverine Zirah (ORCID: https://orcid.org/0000-0001-6082-8414)
- Prem P. Chapagain (ORCID: https://orcid.org/0000-0002-0999-4975)
- Alexander Moiseevich Mebel (ORCID: https://orcid.org/0000-0002-7233-3133)
- Francisco Fernández-Lima (ORCID: https://orcid.org/0000-0002-1283-4390)
- Alain Blond
- Ukesh Karki (ORCID: https://orcid.org/0009-0001-9929-7574)
- Ryane Idir
- Negin Asgharihosseinpour
Institutions
- Centre National de la Recherche Scientifique (FR)
- Florida International University (US)
- Molécules de Communication et Adaptation des Micro-organismes (FR)
- Pharmaceutical Biotechnology (Czechia) (CZ)
- Molecular Research Institute (US)
- Saarland University (DE)
- Technische Universität Braunschweig (DE)
Publication Details
- Journal
- Biochemistry
- Published
- 2026-04-14
- DOI
- https://doi.org/10.1021/acs.biochem.6c00020
- Primary Topic
- Mass Spectrometry Techniques and Applications
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institute of General Medical Sciences