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  • Title: Folding-unfolding of immunoglobulin domains in titin: a simple two-state model.
    Author: Marín JL, Muñiz J, Huerta M, Trujillo X.
    Journal: Gen Physiol Biophys; 1999 Sep; 18(3):305-9. PubMed ID: 10703746.
    Abstract:
    The folding-unfolding reaction rate process in the giant protein titin is studied within a simple two-state model. The molecule is assumed to be stretched by an external force which modulates the potential barrier associated with the folded state. A two-state model for this process is assumed (i.e., the immunoglobulin domains are considered to be either folded or unfolded, with no intermediate states at all). Simple calculations yield a relation between the force and the pulling speed that agrees fairly well with data from experiments and Monte Carlo simulations performed recently. Moreover, in a regime involving ultrafast pulling, the results show that the detailed form of the potential barrier is irrelevant, a conclusion that agrees with the current theoretical work on molecular dynamics.
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