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Showing 1–5 of 5 results
Advanced filters: Author: Jakob P. Ulmschneider Clear advanced filters
  • Insertion of proteins into a membrane bilayer driven by the Sec translocon is aided by the attributes of the inserted peptides. Here, Ulmschneider et al.measure the free energies of various insertion events and suggest that the membrane interface plays an important role in translocon-guided TM helix insertion.

    • Martin B. Ulmschneider
    • Jakob P. Ulmschneider
    • Stephen H. White
    Research
    Nature Communications
    Volume: 5, P: 1-10
  • Many membrane active peptides perforate lipid bilayers. Alamethicin and melittin, two well known examples. Here the authors show that atomic detail simulations can distinguish between equilibrium and transient leakage processes, and predict the detailed pore structures and mechanism of perforation.

    • Jakob P. Ulmschneider
    • Martin B. Ulmschneider
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13
  • Antimicrobial peptides (AMPs) selectively form pores in microbial membranes in process not fully understood. Here the authors use experimentally guided molecular dynamics to study maculatin pore formation, showing how this AMP assembles into transient and structurally diverse oligomeric pores in cell membranes.

    • Yukun Wang
    • Charles H. Chen
    • Jakob P. Ulmschneider
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-9
  • Helicobacter pylori survives in the acidic environment of the stomach by taking up urea and converting it to ammonia and carbon dioxide, which buffer the bacterial periplasm. Using molecular dynamics simulations, McNulty et al. provide insight into the mechanism of urea uptake through the H. pyloriurea transporter.

    • Reginald McNulty
    • Jakob P. Ulmschneider
    • Martin B. Ulmschneider
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-10