Protein design represents one of the great challenges of computational structural biology. The ability to
successfully design new proteins would allow us to generate new reagents and enzymes, while at the same time
providing us with an understanding of the principles of protein stability. Here we report 1H, 15N and 13C
resonance assignments of a redesigned U1A protein, URNdesign. U1A has been studied extensively by our
group and hence was chosen as a design target. For the assignments we sued 2D and 3D heteronuclearNMR
experiments with uniformly 13C, 15N-labeled URNdesign. The assignments for the backbone NH, CO,Ca and
Cb nuclei are 94%complete. Sidechain 1Hand13C, aromatic andQ/NNH2 resonances are essentially complete
with guanidinium and K NH3 residues unassigned. BMRB deposit with accession number 6493
Revised: April 7, 2011 |
Published: October 1, 2005
Citation
Dobson N., G. Dantas, and G. Varani. 2005.1H, 13C and 15N resonance assignments of URNdesign, a computationally redesigned RRM protein.Journal of Biomolecular NMR 33. doi:10.1007/s10858-005-1928-4