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


ABSTRACT: 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.

SUBMITTER: Pande VS 

PROVIDER: S-EPMC17732 | biostudies-literature | 1999 Aug

REPOSITORIES: biostudies-literature

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

Pande V S VS   Rokhsar D S DS  

Proceedings of the National Academy of Sciences of the United States of America 19990801 16


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  ...[more]

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