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. 2007 Aug;33(4):255-70.
doi: 10.1007/s10867-008-9062-7. Epub 2008 Apr 12.

Nonadditive interactions in protein folding: the zipper model of cytochrome C

A N Morozov  1 , Y J Shiu, C T Liang, M Y Tsai, S H Lin
Affiliations

Nonadditive interactions in protein folding: the zipper model of cytochrome C

A N Morozov et al. J Biol Phys. 2007 Aug.

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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References

    1. {'text': '', 'ref_index': 1, 'ids': [{'type': 'DOI', 'value': '10.1103/RevModPhys.71.S419', 'is_inner': False, 'url': 'https://doi.org/10.1103/revmodphys.71.s419'}]}
    2. Frauenfelder, H., Wolynes, P.G., Austin, R.H.: Biological physics. Rev. Mod. Phys. 71, 419–430 (1999)
    1. {'text': '', 'ref_index': 1, 'ids': [{'type': 'DOI', 'value': '10.1146/annurev.physchem.48.1.545', 'is_inner': False, 'url': 'https://doi.org/10.1146/annurev.physchem.48.1.545'}, {'type': 'PubMed', 'value': '9348663', 'is_inner': True, 'url': 'https://pubmed.ncbi.nlm.nih.gov/9348663/'}]}
    2. Onuchic, J.N., Luthey-Schulten, Z., Wolynes, P.G.: Theory of protein folding: the energy landscape perspective. Annu. Rev. Phys. Chem. 48, 545–600 (1997) - PubMed
    1. Levinthal, C.: How to fold graciously. In: Mossbauer Spectroscopy in Biological Systems: Proceedings of the University of Illinois Bulletin, vol. 67, pp. 22–24 (1969)
    1. {'text': '', 'ref_index': 1, 'ids': [{'type': 'DOI', 'value': '10.1073/pnas.89.1.20', 'is_inner': False, 'url': 'https://doi.org/10.1073/pnas.89.1.20'}, {'type': 'PMC', 'value': 'PMC48166', 'is_inner': False, 'url': 'https://pmc.ncbi.nlm.nih.gov/articles/PMC48166/'}, {'type': 'PubMed', 'value': '1729690', 'is_inner': True, 'url': 'https://pubmed.ncbi.nlm.nih.gov/1729690/'}]}
    2. Zwanzig, R., Szabo, A., Bagghi, B.: Levinthal’s paradox. Proc. Natl. Acad. Sci. USA 89, 20–22 (1992) - PMC - PubMed
    1. {'text': '', 'ref_index': 1, 'ids': [{'type': 'DOI', 'value': '10.1002/prot.21080', 'is_inner': False, 'url': 'https://doi.org/10.1002/prot.21080'}, {'type': 'PubMed', 'value': '16894617', 'is_inner': True, 'url': 'https://pubmed.ncbi.nlm.nih.gov/16894617/'}]}
    2. Konermann, L.: Exploring the relationship between funneled energy landscapes and two-state protein folding. Proteins 65, 153–163 (2006) - PubMed

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