ArticleBiophysical journal2011
Role of hydration in collagen recognition by bacterial adhesins.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein Properties.Chemical reviews · 2025Review
- Incubation of Horseradish Peroxidase near 50 Hz AC Equipment Promotes Its Disaggregation and Enzymatic Activity.Micromachines · 2025Article
- Atomic Force Microscopy Study of the Long-Term Effect of the Glycerol Flow, Stopped in a Coiled Heat Exchanger, on Horseradish Peroxidase.Micromachines · 2024Article
- Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Thermal tuning of protein hydration in a hyperthermophilic enzyme.Frontiers in molecular biosciences · 2022Article
- Desolvation of the substrate-binding protein TauA dictates ligand specificity for the alkanesulfonate ABC importer TauABC.The Biochemical journal · 2019Article
- A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Protein science : a publication of the Protein Society · 2018Review
- Dynamic Water-Mediated Hydrogen Bonding in a Collagen Model Peptide.Biochemistry · 2015Article
- Application of sub-micrometer vibrations to mitigate bacterial adhesion.Journal of functional biomaterials · 2014Article
- The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group A Streptococcus shows significant similarity to immunomodulatory HIV protein gp41.The Journal of biological chemistry · 2014Article
- Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses.Biophysical journal · 2013Article
- Polyproline and triple helix motifs in host-pathogen recognition.Current protein & peptide science · 2012Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-protein recognition regulates the vast majority of physiological or pathological processes. We investigated the role of hydration in collagen recognition by bacterial adhesin CNA by means of first principle molecular-dynamics samplings. Our characterization of the hydration properties of the isolated partners highlights dewetting-prone areas on the surface of CNA that closely match the key regions involved in hydrophobic intermolecular interactions upon complex formation, suggesting that the hydration state of the ligand-free CNA predisposes the protein to the collagen recognition. Moreover, hydration maps of the CNA-collagen complex reveal the presence of a number of structured water molecules that mediate intermolecular interactions at the interface between the two proteins. These hydration sites feature long residence times, significant binding free energies, and a geometrical distribution that closely resembles the hydration pattern of the isolated collagen triple helix. These findings are striking evidence that CNA recognizes the collagen triple helix as a hydrated molecule. For this structural motif, the exposure of several unsatisfied backbone carbonyl groups results in a strong interplay with the solvent, which is shown to also play a role in collagen recognition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.