Publications by authors named "M W Kepa"

Traditional root canal therapy (RCT) effectively removes diseased or necrotic pulp tissue and replaces it with inorganic materials. Regenerative endodontics is an alternative to conventional RCT by using biologically based approaches to restore the pulp-dentin complex. This review explores emerging techniques, including autogenic and allogenic pulp transplantation, platelet-rich fibrin, human amniotic membrane scaffolds, specialized pro-resolving mediators, nanofibrous and bioceramic scaffolds, injectable hydrogels, dentin matrix proteins, and cell-homing strategies.

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G protein-coupled receptors (GPCRs) are the largest family of cell surface receptors in humans. The binding and dissociation of ligands tunes the inherent conformational flexibility of these important drug targets towards distinct functional states. Here we show how to trigger and resolve protein-ligand interaction dynamics within the human adenosine A receptor.

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Time-resolved serial crystallography at X-ray Free Electron Lasers offers the opportunity to observe ultrafast photochemical reactions at the atomic level. The technique has yielded exciting molecular insights into various biological processes including light sensing and photochemical energy conversion. However, to achieve sufficient levels of activation within an optically dense crystal, high laser power densities are often used, which has led to an ongoing debate to which extent photodamage may compromise interpretation of the results.

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Article Synopsis
  • X-ray free-electron lasers (XFELs) are advancing time-resolved structural experiments, essential for understanding macromolecule functions and mechanisms.
  • The SwissMX sample-delivery system was tested at SwissFEL using a micro-structured polymer chip, focusing on the light-sensitive protein LOV1 to avoid light contamination during pump-probe experiments.
  • The opaque MISP chips enabled effective studies of LOV1's structural dynamics, confirming a crucial bond formation and suggesting potential for increased XFEL project efficiency by reducing protein sample usage.
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Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs.

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