Paramagnetic tagging of diamagnetic proteins for solution NMR.
In this article, approaches towards the paramagnetic tagging of diamagnetic proteins are reviewed. Alignment can be achieved by adding paramagnetic fusion proteins or peptides to the C- or the N-terminus or by attaching paramagnetic tags to Cystein residues. Applications for the study of homodimer structures and protein/ligand interactions, as well as protein domain dynamics, are reviewed.
Rodriguez-Castañeda
Fernando
F
Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany.
Haberz
Peter
P
Leonov
Andrei
A
Griesinger
Christian
C
D003545:Cysteine / Q000737:chemistry*; D019281:Dimerization; D008024:Ligands; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D008024:Ligands; D011506:Proteins; D003545:Cysteine