Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.

ABSTRACT: Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of globular, modular and intrinsically disordered proteins, as well as protein-protein and protein-DNA complexes. Here we characterized the conformation of a spin-label attached to the homodimeric protein CylR2 using a combination of X-ray crystallography, electron paramagnetic resonance (EPR) and NMR spectroscopy. Close agreement was found between the conformation of the spin label observed in the crystal structure with interspin distances measured by EPR and signal broadening in NMR spectra, suggesting that the conformation seen in the crystal structure is also preferred in solution. In contrast, c

SUBMITTER: Gruene T 

PROVIDER: S-EPMC3042103 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature