Paramagnetic effects provide unique information about the structure and dynamics of biomolecules. We developed a method in which the lanthanoid tag is not directly attached to the protein of interest, but instead to a "reporter" protein, which binds and then transmits paramagnetic information to the target. The designed method allows access to a large number of paramagnetic restraints and residual dipolar couplings produced from independent molecular alignments in high-molecular-weight proteins with unknown 3D structure.

Multiple paramagnetic effects through a tagged reporter protein

Munari, Francesca;
2015-01-01

Abstract

Paramagnetic effects provide unique information about the structure and dynamics of biomolecules. We developed a method in which the lanthanoid tag is not directly attached to the protein of interest, but instead to a "reporter" protein, which binds and then transmits paramagnetic information to the target. The designed method allows access to a large number of paramagnetic restraints and residual dipolar couplings produced from independent molecular alignments in high-molecular-weight proteins with unknown 3D structure.
2015
NMR spectroscopy; lanthanoids; paramagnetism; proteins; structural biology; Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Escherichia coli; Humans; Lanthanoid Series Elements; Maltose-Binding Proteins; Models, Molecular; Protein Structure, Tertiary; Proteins; Ubiquitin; Nuclear Magnetic Resonance, Biomolecular
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11562/973478
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