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Nonadditive Interactions in Protein Folding: The Zipper Model of Cytochrome c

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Abstract

Hydrogen exchange experiments (Krishna et al. in J. Mol. Biol. 359:1410, 2006) reveal that folding–unfolding of cytochrome c occurs along a defined pathway in a sequential, stepwise manner. The simplified zipper-like model involving nonadditive coupling is proposed to describe the classical “on pathway” folding–unfolding behavior of cytochrome c. Using free energy factors extracted from HX experiments, the model can predict and explain cytochrome c behavior in spectroscopy studies looking at folding equilibria and kinetics. The implications of the proposed model are discussed for such problems as classical pathway vs. energy landscape conceptions, structure and function of a native fold, and interplay of secondary and tertiary interactions.

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Authors and Affiliations

  1. Institute of Atomic and Molecular Sciences, Academia Sinica, P.O. Box 23-166, Taipei, Taiwan, Republic of China

    A. N. Morozov, Y. J. Shiu, C. T. Liang & M. Y. Tsai

  2. National Chiao Tung University, 1001 Ta Hsuen Road, Hsinchu, Taiwan, Republic of China

    S. H. Lin

  3. Institute of Surface Chemistry, National Academy of Sciences of Ukraine, Generala Naumova str. 17, Kyiv, 03164, Ukraine

    A. N. Morozov

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  1. A. N. Morozov
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  2. Y. J. Shiu
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  3. C. T. Liang
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  4. M. Y. Tsai
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Correspondence to A. N. Morozov.

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Morozov, A.N., Shiu, Y.J., Liang, C.T. et al. Nonadditive Interactions in Protein Folding: The Zipper Model of Cytochrome c . J Biol Phys 33, 255–270 (2007). https://doi.org/10.1007/s10867-008-9062-7

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  • DOI: https://doi.org/10.1007/s10867-008-9062-7

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