Abstract
A method of Mössbauer Fourier spectroscopy is developed to determine the correlation function of coordinates of a macromolecular system. The method does not require the use of an a priori dynamic model. The application of the method to the analysis of RSMR data for human serum albumin has demonstrated considerable changes in the dynamic behavior of the protein globule when the temperature is changed from 270 to 310 K. The main conclusions of the present work is the simultaneous observation of low-frequency (τ≥10−9 sec) and high-frequency (τ≪10−9 sec) large-scaled motions, that is the two-humped distribution of correlation times of protein motions.
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Basovets, S.K., Uporov, I.V., Shaitan, K.V. et al. A method of mössbauer fourier spectroscopy for determination of the biopolimer coordinate correlation functions. Hyperfine Interact 39, 369–378 (1988). https://doi.org/10.1007/BF02397646
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DOI: https://doi.org/10.1007/BF02397646