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Mu Gao, Hui Lu, and Klaus Schulten. Simulated refolding of stretched titin immunoglobulin domains. Biophysical Journal, 81:2268-2277, 2001. Steered Molecular Dynamics (SMD) is used to investigate forced unfolding and spontaneous refolding of immunoglobulin I27, a domain of the muscle protein titin. Previous SMD simulations revealed the events leading to stretch-induced unfolding of I27, the rupture of hydrogen bonds bridging $\beta$-strands A and B and bridging $\beta$-strands A' and G, corresponding to an extension of $\sim$15 Å and preceding the complete unfolding. The method is now employed to study the refolding of partially unfolded I27 domains. The simulations revealed that stretched domains with ruptured interstrand hydrogen bonds shrank along the extension direction. Two types of refolding patterns were recognized: five of the six hydrogen bonds between $\beta$-strands A' and G reform in less than 200 ps, whereas hydrogen bonds between $\beta$-strands A and B do not exhibit stable reformation on a 2 ns time scale. The mechanical stability of the partially refolded intermediates was tested by restretching. Full Text

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