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- W2112918439 abstract "Using a specifically designed Go-model we have performed all-atom simulations of the C-fragment of TOP7. Our results support previous results (see Mohanty S. et al., Proc. Natl. Acad. Sci. U.S.A., 105 (2008) 8004; Mohanty S. and Hansmann U. H. E., J. Phys. Chem. B, 112 (2008) 15134) that indicate folding of this protein through configurations with non-native secondary structure. The N-terminal residues form first an extension of a subsequent ?-helix, before finally refolding into a ?-strand that completes a three-stranded ?-sheet in the final structure. We show that mutations which reduce the chameleonicity of N-terminal residues (by increasing the propensity for strandness and reducing that for helicity) lead to folding into the same structure but with reduced folding rates and larger free-energy barriers." @default.
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- W2112918439 date "2012-03-01" @default.
- W2112918439 modified "2023-10-04" @default.
- W2112918439 title "Chameleonicity and folding of the C-fragment of TOP7" @default.
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- W2112918439 doi "https://doi.org/10.1209/0295-5075/97/68003" @default.
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