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Electron Correlation in Quantum Molecular Biophysics: The Case Study of Hemocyanin

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Part of the book series: Electronics and Biotechnology Advanced (EL.B.A.) Forum Series ((ELBA,volume 3))

Abstract

One of the most interesting problems of modern molecular biophysics is the study of the relationship between structure and function in proteins. The data base of proteins known at atomic resolutions (the Brookhaven Protein Data Base (PDB), release 19/9/1997) presently comprises 5900 structures, obtained from X ray diffraction patterns of ordered crystals or in some cases from twodimensional NMR spectroscopy. Well resolved structures include enzymes of several different type.

The underlying physical laws necessary for the mathematical theory of a large part of physics and the whole of chemistry are thus completely known, and the difficulty is only that the exact application of these laws leads to equations much too complicated to be soluble.

— P. A. M. DIRAC, 1929

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Fariselli, P., Casadio, R. (1998). Electron Correlation in Quantum Molecular Biophysics: The Case Study of Hemocyanin. In: Nicolini, C. (eds) Biophysics of Electron Transfer and Molecular Bioelectronics. Electronics and Biotechnology Advanced (EL.B.A.) Forum Series, vol 3. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9516-5_8

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  • DOI: https://doi.org/10.1007/978-1-4757-9516-5_8

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9518-9

  • Online ISBN: 978-1-4757-9516-5

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