Abstract
Herein, a novel and rationally designed ortho-substituted pyridine activator is reported that reacts rapidly and selectively with cysteine thiols. It forms reduction-stable conjugates and induces large pseudocontact shifts, residual dipolar couplings and paramagnetic relaxation enhancement on both ubiquitin S57C and human carbonic anhydrase II S50C constructs under physiological conditions.
MeSH terms
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Alkylation
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Anisotropy
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Carbonic Anhydrase II / chemistry*
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Chelating Agents / chemistry*
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Coordination Complexes / chemistry*
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Cysteine / chemistry
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Humans
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Indicators and Reagents / chemistry*
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Lanthanoid Series Elements / chemistry*
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular / methods*
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Oxidation-Reduction
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Protein Conformation
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Pyridines / chemistry
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Sulfhydryl Compounds / chemistry
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Ubiquitin / chemistry
Substances
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Chelating Agents
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Coordination Complexes
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Indicators and Reagents
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Lanthanoid Series Elements
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Pyridines
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Sulfhydryl Compounds
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Ubiquitin
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Carbonic Anhydrase II
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CA2 protein, human
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Cysteine
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pyridine