Send to

Choose Destination
See comment in PubMed Commons below
J Biol Phys. 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.

Author information

Institute of Atomic and Molecular Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.


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.

PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer Icon for PubMed Central
    Loading ...
    Support Center