ArticleEuropean biophysics journal : EBJ2011
An alternative flexible conformation of the E. coli HUβ₂ protein: structural, dynamics, and functional aspects.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Consensus protein engineering on the thermostable histone-like bacterial protein HUs significantly improves stability and DNA binding affinity.Extremophiles : life under extreme conditions · 2020Article
- Liquid Native MALDI Mass Spectrometry for the Detection of Protein-Protein Complexes.Journal of the American Society for Mass Spectrometry · 2018Article
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Authors and funding
7 authors.
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Abstract
The histone-like HU protein is the major nucleoid-associated protein involved in the dynamics and structure of the bacterial chromosome. Under physiological conditions, the three possible dimeric forms of the E. coli HU protein (EcHUα₂, EcHUβ₂, and EcHUαβ) are in thermal equilibrium between two dimeric conformations (N₂ ↔ I₂) varying in their secondary structure content. High-temperature molecular dynamics simulations combined with NMR experiments provide information about structural and dynamics features at the atomic level for the N₂ to I₂ thermal transition of the EcHUβ₂ homodimer. On the basis of these data, a realistic 3D model is proposed for the major I₂ conformation of EcHUβ₂. This model is in agreement with previous experimental data.
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