ArticleThe journal of physical chemistry. B2024
Molecular Dynamics Investigation of the Influenza Hemagglutinin Conformational Changes in Acidic pH.
Article in The journal of physical chemistry. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structural vaccinology expedites rational design of next-generation vaccines for influenza and respiratory syncytial virus.Virologica Sinica · 2026Review
- Integrating Molecular Dynamics Simulations and Single-molecule FRET Spectroscopy: From Computational FRET Estimation to Experimental Data Interpretation.The journal of physical chemistry. B · 2026Review
- Structural dynamics of sphingosine kinase 1 regulation and inhibition.bioRxiv : the preprint server for biology · 2025Article
- Structural dynamics of sphingosine kinase 1 regulation and inhibition.Research square · 2025Article
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3 authors.
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Abstract
The surface protein hemagglutinin (HA) of the influenza virus plays a pivotal role in facilitating viral infection by binding to sialic acid receptors on host cells. Its conformational state is pH-sensitive, impacting its receptor-binding ability and evasion of the host immune response. In this study, we conducted extensive equilibrium microsecond-level all-atom molecular dynamics (MD) simulations of the HA protein to explore the influence of low pH on its conformational dynamics. Specifically, we investigated the impact of protonation on conserved histidine residues (H106
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