Publication | Closed Access
Tyrosine‐Targeted Spin Labeling and EPR Spectroscopy: An Alternative Strategy for Studying Structural Transitions in Proteins
52
Citations
18
References
2011
Year
Protein ChemistryUnique Tyrosine ResidueSpin LabelingProtein AssemblyBiochemistryProtein FoldingHigh MobilityNatural SciencesProtein X-ray CrystallographyMolecular BiologyEpr SpectroscopyCp12 ProteinProtein NmrMedicineStructural TransitionsStructural Biology
Keeping tabs on tyrosine: A three-component Mannich-type reaction extends the scope of site-directed spin labeling by selectively labeling the unique tyrosine residue of CP12 protein (see picture), as was confirmed by mass spectrometry. EPR spectroscopy of the labeled protein showed a very high mobility of the probe, which remained very mobile after complex formation with GAPDH.
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