Publications by authors named "Daria D Kuklina"
Article Synopsis
- Ferritin-based hybrids are large macromolecules with potential uses in drug delivery and vaccines, but their design is complicated.
- Researchers designed hybrids using ferritin from Helicobacter pylori and a Small Ubiquitin-like Modifier, discovering that their assembly was influenced by varying preparation methods.
- They developed a quantitative model to analyze how different stoichiometries affected the structure of these hybrids, revealing unexpected patterns and establishing a framework for better design of ferritin-based systems.
Article Synopsis
- β-carotene (BCR) is a key carotenoid that acts as a colorant, antioxidant, and provitamin A, but its hydrophobic nature makes it challenging to distribute in water.
- The crystal structure of a BCR-binding protein (BBP) from male locusts reveals how this protein efficiently binds BCR, forming a unique tubular structure that accommodates the carotenoid.
- BBP can also bind various xanthophylls depending on their oxygen content but does not bind lycopene, highlighting its potential use in solubilizing BCR for applications.
Article Synopsis
- Actin exists in three forms: monomeric globular (G-actin), polymeric fibrillar (F-actin), and an inactivated form called I-actin, which forms without cellular folding machinery.
- The transformation from G-actin to I-actin can occur through various methods, including removal of divalent ions, mild denaturants, or heat, and I-actin can aggregate into oligomers of about 14-16 G-actin monomers.
- This study uses small-angle X-ray scattering to investigate the oligomerization process of I-actin, distinguishing it from F-actin and revealing a unique pathway of oligomer formation.
F-type ATP synthases play a key role in oxidative and photophosphorylation processes generating adenosine triphosphate (ATP) for most biochemical reactions in living organisms. In contrast to the mitochondrial FF-ATP synthases, those of chloroplasts are known to be mostly monomers with approx. 15% fraction of oligomers interacting presumably non-specifically in a thylakoid membrane.
View Article and Find Full Text PDFFerritin is a vital protein complex responsible for storing iron in almost all living organisms. It plays a crucial role in various metabolic pathways, inflammation processes, stress response, and pathogenesis of cancer and neurodegenerative diseases. In this review we discuss the role of ferritin in diseases, cellular iron regulation, its structural features, and its role in biotechnology.
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