ArticleBiophysical journal2011
Modelling of lysozyme binding to a cation exchange surface at atomic detail: the role of flexibility.
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.
- The Effects of pH on Orientations of Adsorbed Lysozyme on Negatively Charged Surfaces.The journal of physical chemistry. B · 2026Article
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- Surface plasmon resonance, molecular docking, and molecular dynamics simulation studies of lysozyme interaction with tannic acid.Food science & nutrition · 2024Article
- Influence of chirality and sequence in lysine-rich lipopeptide biosurfactants and micellar model colloid systems.Nature communications · 2024Article
- Anionic Hyperbranched Amphiphilic Polyelectrolytes as Nanocarriers for Antimicrobial Proteins and Peptides.Materials (Basel, Switzerland) · 2023Article
- Hemocompatibility of β-Cyclodextrin-Modified (Methacryloyloxy)ethyl Phosphorylcholine Coated Magnetic Nanoparticles.Biomolecules · 2023Article
- Hyperbranched Copolymers of Methacrylic Acid and Lauryl Methacrylate H-P(MAA-co-LMA): Synthetic Aspects and Interactions with Biorelevant Compounds.Pharmaceutics · 2023Article
- Hyperbranched Polyelectrolyte Copolymers as Novel Candidate Delivery Systems for Bio-Relevant Compounds.Materials (Basel, Switzerland) · 2023Article
- Imbalance of peptidoglycan biosynthesis alters the cell surface charge ofCell surface (Amsterdam, Netherlands) · 2022Article
- Article
- Lysozyme-Responsive Spray-Dried Chitosan Particles for Early Detection of Wound Infection.ACS applied bio materials · 2019Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Different approaches were made to predict the adsorbed orientation based on rigid, flexible, or a mixture of both models. To determine the role of flexibility during adsorption, the orientation of lysozyme adsorbed to a negatively charged ligand surface was predicted by a rigid and a flexible model based on two differing protein structures at atomic resolution. For the rigid model, the protein structures were placed at different distances from the ligand surface and the electrostatic interaction energy was calculated for all possible orientations. The results were compared to a flexible model where the binding to the ligand surface was modeled by multiple molecular dynamics simulations starting with 14 initial orientations. Different aspects of the adsorption process were not covered by the rigid model and only detectable by the flexible model. Whereas the results of the rigid model depended sensitively on the protein-surface distance and the protein structure, the preferred orientation obtained by the flexible model was closer to a previous experimental determined orientation, robust toward the initial orientation and independent of the initial protein structure. Additionally, it was possible to obtain insights into the preferred binding process of lysozyme on a negatively charged surface by the flexible model.
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