Publications by authors named "C Betzel"
Growing a single suspended perfect protein crystal in a fully noncontact manner.
Int J Biol Macromol
December 2024
Article Synopsis
- * The study presents a novel technique for controlling protein crystal nucleation using magnetic forces, specifically by adding paramagnetic salt to the solution.
- * This method allows for the confinement of nucleation to a single crystal nucleus without direct contact, which improves crystal quality by reducing nucleation and growth rates through minimized convection.
The "green synthesis" of nanoparticles (NPs) offers cost-effective and environmentally friendly advantages over chemical synthesis by utilizing biological sources such as bacteria, algae, fungi, or plants. In this context, cyanobacteria and their components are valuable sources to produce various NPs. The present study describes the comparative analysis of physicochemical and antibacterial properties of chemically synthesized (Chem-AgNPs) and cyanobacteria -derived silver NPs (Splat-AgNPs).
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- * Recent advancements in the field include the approval of boronate-based β-lactamase inhibitors for treating multidrug-resistant bacteria, emphasizing the need for effective solutions.
- * Researchers used time-resolved serial crystallography to gain insights into the binding mechanisms of β-lactamase CTX-M-14, collecting detailed data that enhances the understanding of enzymatic reactions and resistance.
Infectious diseases are a significant cause of death, and recent studies estimate that common bacterial infectious diseases were responsible for 13.6% of all global deaths in 2019. Among the most significant bacterial pathogens is Staphylococcus aureus, accounting for more than 1.
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- The main protease (M) of SARS-CoV-2 is crucial for the virus's functionality and is considered a potential target for drug development, as it is only active in its reduced form.
- When oxidized, M's activity halts but can be restored, indicating an evolutionary adaptation to oxidative environments, although the protective mechanisms haven't been fully elucidated.
- Researchers determined the crystal structure of oxidized M, revealing a disulfide bond that affects its dimer stability and crystallization, providing insights into the protein's response to oxidative stress and its structural study conditions.*