Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins.
作者： Philippe S. Nadaud , Jonathan J. Helmus , Stefanie L. Kall , Christopher P. Jaroniec
DOI: 10.1021/JA900224Z
关键词: Crystallography 、 Quantum number 、 Solid-state nuclear magnetic resonance 、 Protein G 、 Side chain 、 Ion 、 Paramagnetism 、 Diamagnetism 、 Relaxation (NMR) 、 Chemistry
摘要: Magic-angle-spinning solid-state nuclear magnetic resonance (SSNMR) studies of natively diamagnetic uniformly 13C,15N-enriched proteins, intentionally modified with side chains containing paramagnetic ions, are presented, the aim using concomitant relaxation enhancements (PREs) as a source long-range structural information. The ions incorporated at selected sites in protein EDTA−metal complexes by introducing solvent-exposed cysteine residue site-directed mutagenesis, followed modification thiol-specific reagent, N-[S-(2-pyridylthio)cysteaminyl]EDTA-metal. Here, this approach is demonstrated for K28C and T53C mutants B1 immunoglobulin-binding domain G (GB1), EDTA-Mn2+ EDTA-Cu2+ chains. It shown that incorporation moieties, exhibiting different times spin quantum numbers, facilitates convenient modulation longitudinal (R1) transverse (R2, R1ρ) r...
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