Backbone Torsion Angle Determination Using Proton Detected Magic-Angle Spinning Nuclear Magnetic Resonance.
Kai XueEvgeny NimerovskyKumar A Tekwani MovellanStefan BeckerLoren B AndreasPublished in: The journal of physical chemistry letters (2021)
Protein torsion angles define the backbone secondary structure of proteins. Magic-angle spinning (MAS) NMR methods using carbon detection have been developed to measure torsion angles by determining the relative orientation between two anisotropic interactions─dipolar coupling or chemical shift anisotropy. Here we report a new proton-detection based method to determine the backbone torsion angle by recoupling NH and CH dipolar couplings within the HCANH pulse sequence, for protonated or partly deuterated samples. We demonstrate the efficiency and precision of the method with microcrystalline chicken α spectrin SH3 protein and the influenza A matrix 2 (M2) membrane protein, using 55 or 90 kHz MAS. For M2, pseudo-4D data detect a turn between transmembrane and amphipathic helices.
Keyphrases
- high resolution
- magnetic resonance
- solid state
- room temperature
- loop mediated isothermal amplification
- amino acid
- protein protein
- real time pcr
- blood pressure
- label free
- magnetic resonance imaging
- small molecule
- contrast enhanced
- binding protein
- sensitive detection
- living cells
- fluorescent probe
- tandem mass spectrometry
- quantum dots
- single molecule