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Higher Order Correlations in Proteins by X-Ray Spectroscopy

  • Conference paper
Biophysics and Synchrotron Radiation

Part of the book series: Springer Series in Biophysics ((BIOPHYSICS,volume 2))

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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Author information

Authors and Affiliations

  1. Dipartimento di Fisica, Università degli Studi di Roma “La Sapienza”, 00185, Roma, Italy

    A. Bianconi

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  1. A. Bianconi
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Editors and Affiliations

  1. Department of Physics, University of Rome, “La Sapienza” Piazzale Aldo Moro, 2, I-00185, Rome, Italy

    Antonio Bianconi  & Agostina Congiu Castellano  & 

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© 1987 Springer-Verlag Berlin Heidelberg

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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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  • DOI: https://doi.org/10.1007/978-3-642-71490-0_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-71492-4

  • Online ISBN: 978-3-642-71490-0

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