Article
Structural characterization of the Cu(II)-NTA spin label on α-helices by X-ray crystallography and electron paramagnetic resonance.
Structure (London, England : 1993) - 2 Apr 2026
Besaw Jessica E, Reichenwallner Jörg, Chen Evelyn Y, Hermet-Teesalu Paule, Tregubenko Anastassiya, Kim Kyumhyuk, Morizumi Takefumi, Ustav Mart, Ernst Oliver P
Abstract excerpt
Site-directed Cu(II)-labelling in pulsed electron paramagnetic resonance (EPR) spectroscopy has demonstrated narrow Cu(II)-Cu(II) distance distributions suitable to resolve subtle protein conformational changes. The high precision derives from a double histidine (dHis) mutation that effectively locks a Cu(II)-nitrilotriacetic acid (Cu(II)-NTA) moiety in place. To date, no structures featuring the dHis-Cu(II)-NTA...
Topics
- Electron Spin Resonance Spectroscopy
- Crystallography, X-Ray
- Muramidase
- Copper
- Spin Labels
- Models, Molecular
- Nitrilotriacetic Acid
- Protein Conformation, alpha-Helical
- Histidine
- Bacteriophage T4
- Binding Sites
- Mutation