Intramolecular electron transfer in lysozyme studied by time-resolved chemically induced dynamic nuclear polarization.

Journal article

The kinetics of the chemically induced dynamic nuclear polarization (CIDNP) produced in reactions of hen lysozyme with photosensitizers have been studied for the native state of the protein at pH 3.8 and for two denatured states. The latter were generated by raising the temperature to 80 degrees C or by combining a temperature rise (to 50 degrees C) with the addition of chemical denaturant (10 M urea). Detailed analysis of the CIDNP time dependence on a microsecond time scale revealed that, i...

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Authors: Morozova, O; Hore, P; Sagdeev, R; Yurkovskaya, A

• Publication status: Published
• Journal: journal of physical chemistry. B
• Volume: 109
• Issue: 46
• Pages: 21971-21978
• Publication date: 2005-11-01
• DOI: 10.1021/jp053394v
• EISSN: 1520-5207
• ISSN: 1520-6106
• Language: English
• Keywords: Photochemistry; Time Factors; Reference Standards; Magnetic Resonance Spectroscopy; Hydrogen-Ion Concentration; Sensitivity and Specificity; Animals; Kinetics; Temperature; Chickens; Electrons; Protein Structure, Secondary; Protein Conformation; Muramidase