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- W1517333547 abstract "Cytochrome c has become a paradigm for protein folding and electron transfer studies, because of its stability, solubility, and ease of preparation. This chapter describes the high-resolution solution structures for ferro- and ferricytochrome c, using 1H 2D and 3D NMR spectroscopy and hybrid distance geometry, simulated annealing calculations. The solution structures of horse ferro- and ferricytochrome c to high resolution are determined using a comprehensive battery of 1H-based NMR experiments, including three dimensional homonuclear spectra, and the key to this approach is the use of advanced statistical methods to compensate for the lack of extensive torsion angle constraints in the identification of prochiral hydrogens. The use of three dimensional spectroscopy in conjunction with good working models of the structures has allowed the number of NOE-based restraints that could be determined to approach the density required for high resolution structures to be obtained. The chapter suggests that these detailed structural studies will provide the basis for a comprehensive re-evaluation of hypotheses, concerning the fundamental nature of the electron transfer processes in proteins and also serves to illustrate that highly defined molecular models of proteins of moderate size can be determined using structural restraints derived solely from 1H NMR experiments." @default.
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- W1517333547 date "1995-01-01" @default.
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- W1517333547 title "Solution structures of horse ferro- and ferricytochrome c using 2D and 3D 1H NMR and restrained simulated annealing" @default.
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- W1517333547 doi "https://doi.org/10.1016/s1080-8914(06)80062-1" @default.
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