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Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):9062-7.

Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G.

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Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.


We have studied the unfolding and refolding pathway of a beta-hairpin fragment of protein G by using molecular dynamics. Although this fragment is small, it possesses several of the qualities ascribed to small proteins: cooperatively formed beta-sheet secondary structure and a hydrophobic "core" of packed side chains. At high temperatures, we find that the beta-hairpin unfolds through a series of sudden, discrete conformational changes. These changes occur between states that are identified with the folded state, a pair of partially unfolded kinetic intermediates, and the unfolded state. To study refolding at low temperatures, we perform a series of short simulations starting from the transition states of the discrete transitions determined by the unfolding simulations.

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