Improved photo-CIDNP methods for studying protein structure and folding.

Journal article

Two new techniques offering considerable improvements in the quality of 1H photo-CIDNP spectra of proteins are demonstrated. Both focus on the problem of progressive photo-degradation of the flavin dye used to generate polarization in exposed tryptophan, tyrosine and histidine side-chains. One approach uses rapid addition and removal of protein/flavin solution between light flashes to mix the NMR sample and introduce fresh dye into the laser-irradiated region. The other involves chemical oxid...

Expand abstract

Authors: Maeda, K; Lyon, C; Lopez, J; Cemazar, M; Dobson, C

• Publication status: Published
• Journal: Journal of biomolecular NMR
• Volume: 16
• Issue: 3
• Pages: 235-244
• Publication date: 2000-03-01
• DOI: 10.1023/a:1008351128089
• EISSN: 1573-5001
• ISSN: 0925-2738
• Language: English
• Keywords: Tryptophan; Light; Hydrogen Peroxide; Protein Folding; Flavins; Animals; Tyrosine; Cattle; Lactalbumin; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Histidine