ausblenden:
Schlagwörter:
paramagnetic relaxation enhancement, MTSL spin label, solid-state NMR spectroscopy, protein structure determination
Zusammenfassung:
Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy has been used successfully to elucidate atomic-resolution structures of insoluble proteins. However, the major bottleneck is the difficulty to obtain valuable long-distance structural information. Here we propose to use distance restraints as long as 32 Å obtained from quantification of transverse proton relaxation induced by a methanethiosulfonate spin label (MTSL). Combined with dipolar proton-proton distance restraints, we are able to obtain a protein structure with excellent precision from a single spin-labeled protein sample of an amount of 1 mg under fast magic angle spinning.
