A5048609580- Lipid Membrane Structure and Behavior
- Surfactants and Colloidal Systems
- Ion Transport and Channel Regulation
- Spectroscopy and Quantum Chemical Studies
- Receptor Mechanisms and Signaling
- Bacteriophages and microbial interactions
- Antimicrobial Peptides and Activities
- Erythrocyte Function and Pathophysiology
- Characterization and Applications of Magnetic Nanoparticles
- Connexins and lens biology
Universidad de Los Andes
2023-2024
Heidelberg Institute for Theoretical Studies
2024
Biogen (United States)
2024
Arizona State University
2024
Rockefeller University
2024
Harvard University
2024
Universidad de Los Andes
2021-2023
Universidad Nacional de Colombia
2014
Aquaporin-0 (AQP0) tetramers form square arrays in lens membranes through a yet unknown mechanism, but are enriched sphingomyelin and cholesterol. Here, we determined electron crystallographic structures of AQP0 sphingomyelin/cholesterol performed molecular dynamics (MD) simulations to establish that the observed cholesterol positions represent those seen around an isolated tetramer largely defines location orientation most its associated molecules. At high concentration, increases...
Several antimicrobial peptides, including magainin and the human cathelicidin LL‐37, act by forming pores in bacterial membranes. Bacteria such as Staphylococcus aureus modify their membrane's cardiolipin composition to resist types of perturbations that compromise membrane stability. Here, we used molecular dynamic simulations quantify role on formation simple bacterial‐like models composed phosphatidylglycerol mixtures. Cardiolipin modified structure ordering lipid bilayer, making it less...
Aquaporin-0 (AQP0) tetramers form square arrays in lens membranes through a yet unknown mechanism, but are enriched sphingomyelin and cholesterol. Here, we determined electron crystallographic structures of AQP0 sphingomyelin/cholesterol performed molecular dynamics (MD) simulations to establish that the observed cholesterol positions represent those seen around an isolated tetramer largely defines location orientation most its associated molecules. At high concentration, increases...
Aquaporin-0 (AQP0) tetramers form square arrays in lens membranes through a yet unknown mechanism, but are enriched sphingomyelin and cholesterol. Here, we determined electron crystallographic structures of AQP0 sphingomyelin/ cholesterol performed molecular dynamics (MD) simulations to establish that the observed positions represent those seen around an isolated tetramer largely defines location orientation most its associated molecules. At high concentration, increases hydrophobic...
Aquaporin-0 (AQP0) tetramers form square arrays in lens membranes through a yet unknown mechanism, but are enriched sphingomyelin and cholesterol. Here, we determined electron crystallographic structures of AQP0 sphingomyelin/cholesterol performed molecular dynamics (MD) simulations to establish that the observed cholesterol positions represent those seen around an isolated tetramer largely defines location orientation most its associated molecules. At high concentration, increases...
Aquaporin-0 (AQP0) tetramers form square arrays in lens membranes through a yet unknown mechanism, but are enriched sphingomyelin and cholesterol. Here, we determined electron crystallographic structures of AQP0 sphingomyelin/cholesterol performed molecular dynamics (MD) simulations to establish that the observed cholesterol positions represent those seen around an isolated tetramer largely defines location orientation most its associated molecules. At high concentration, increases...
Withdrawal Statement The authors have withdrawn this manuscript owing to its merge with BIORXIV/2023/540959. Therefore, the do not wish work be cited as reference for project. If you any questions, please contact corresponding author. merged preprint can found at doi.org/10.1101/2023.05.16.540959