Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite. J Struct Biol 2024 Mar;216(1):108061
Date
01/08/2024Pubmed ID
38185342Pubmed Central ID
PMC10939839DOI
10.1016/j.jsb.2024.108061Scopus ID
2-s2.0-85182378487 (requires institutional sign-in at Scopus site)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.
Author List
Gopinath T, Shin K, Tian Y, Im W, Struppe J, Perrone B, Hassan A, Marassi FMAuthors
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinKyungsoo Shin PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
Gopinath Tata PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
DurapatiteHumans
Magnetic Resonance Imaging
Magnetic Resonance Spectroscopy
Nuclear Magnetic Resonance, Biomolecular
Vitronectin
