Protein conformation from electron spin relaxation data.

James Paul Allen, J. T. Colvin, D. G. Stinson, C. P. Flynn, H. J. Stapleton

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Electron spin relaxation data from five ferric proteins are analyzed in terms of the fractal model of protein structures. Details of this model are presented. The results lead to a characterization of protein structures by a single parameter, the fractal dimension, d. This structural parameter is shown to determine the temperature dependence of the Raman electron spin relaxation rate, which varies as T3 + 2d. Computations of d are made using x-ray data for 17 proteins. The results range from d = 1.76 for lysozyme to d = 1.34 for ferredoxin. These values are compared with values of d obtained from the present electron spin relaxation data on five ferric proteins. Typical results are d = 1.34 +/- 0.06 from relaxation data and 1.34 +/- 0.05 from x-ray data for ferredoxin; d = 1.67 +/- 0.03 from relaxation data and 1.66 +/- 0.05 from x-ray data for ferricytochrome c. The data thus support the theoretical model. Applications of this spin resonance technique to the study of changes in protein conformation are discussed.

Original languageEnglish
Pages (from-to)299-310
Number of pages12
JournalBiophysical Journal
Issue number3
Publication statusPublished - Jun 1982

ASJC Scopus subject areas

  • Biophysics

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    Allen, J. P., Colvin, J. T., Stinson, D. G., Flynn, C. P., & Stapleton, H. J. (1982). Protein conformation from electron spin relaxation data. Biophysical Journal, 38(3), 299-310.