Abstract
EXAFS (Extended X-ray absorption Fine Structure) has been used to measure the interatomic distances of active sites of proteins because it probes the pair distribution function, i. e. the first order correlation function of local atomic distribution, since the beginning of x-ray spectroscopy of biological molecules(1–4) and it is currently used to investigate metalloproteins(5–9). It was pointed out that the x-ray absorption spectra of biological molecules can give information on site geometry by switching the focus of the data analysis from the EXAFS region to the XANES (X-ray Absorption Near Edge Structure) region(10–13).
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Bianconi, A. (1987). Higher Order Correlations in Proteins by X-Ray Spectroscopy. In: Bianconi, A., Congiu Castellano, A. (eds) Biophysics and Synchrotron Radiation. Springer Series in Biophysics, vol 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71490-0_10
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