ArticleJournal of structural biology2024
Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite.
Article in Journal of structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Review
- MAS Cryoprobe Enhances Solid-State NMR Signals of α-Synuclein Fibrils.bioRxiv : the preprint server for biology · 2025Article
- 3D-Printed Device for Efficient Packing of Semisolid Samples in 3.2-mm Rotors Used in Cryoprobe Systems.Magnetic resonance in chemistry : MRC · 2025Article
- Potential urinary volatile organic compounds as screening markers in cancer - a review.Frontiers in oncology · 2024Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
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Abstract
The low sensitivity of nuclear magnetic resonance (NMR) is a major bottleneck for studying biomolecular structures of complex biomolecular assemblies. Cryogenically cooled probe technology overcomes the sensitivity limitations enabling NMR applications to challenging biomolecular systems. Here we describe solid-state NMR studies of the human blood protein vitronectin (Vn) bound to hydroxyapatite (HAP), the mineralized form of calcium phosphate, using a CryoProbe designed for magic angle spinning (MAS) experiments. Vn is a major blood protein that regulates many different physiological and pathological processes. The high sensitivity of the CryoProbe enabled us to acquire three-dimensional solid-state NMR spectra for sequential assignment and characterization of site-specific water-protein interactions that provide initial insights into the organization of the Vn-HAP complex. Vn associates with HAP in various pathological settings, including macular degeneration eyes and Alzheimer's disease brains. The ability to probe these assemblies at atomic detail paves the way for understanding their formation.
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