Evolutionary diversity and structural dynamics of the outer membrane protein Ail in <i>Yersinia</i>
Ail, their potential influence on structural dynamics as well as intrinsic disorder predisposition of this protein. The natural polymorphism is restricted to functionally important loops. We use molecular dynamics simulations and intrinsic disorder predictions to assess how these polymorphisms affect Ail conformational dynamics, revealing that minor sequence divergences correlate with distinst dynamic profiles indicating isoform-specific modulation of Ail function.
Authors
- Angelina A. Kislichkina (ORCID: https://orcid.org/0000-0001-8389-2494)
- Jesper J. Madsen (ORCID: https://orcid.org/0000-0003-1411-9080)
- Svetlana V. Dentovskaya (ORCID: https://orcid.org/0000-0002-1996-8949)
- Andrey P. Anisimov (ORCID: https://orcid.org/0000-0002-5499-7999)
- Vladimir Nikolaevich Uversky (ORCID: https://orcid.org/0000-0002-4037-5857)
Institutions
- University of South Florida (US)
- State Research Center for Applied Microbiology and Biotechnology (RU)
- USF Health Byrd Alzheimer's Institute (US)
Publication Details
- Journal
- Journal of Biomolecular Structure and Dynamics
- Published
- 2026-04-16
- DOI
- https://doi.org/10.1080/07391102.2026.2642917
- Primary Topic
- Yersinia bacterium, plague, ectoparasites research
- Type
- article
- Field-Weighted Citation Impact
- 0.00