Chameleonicity and folding of the C-fragment of TOP7
Document Type
Article
Publication Date
3-1-2012
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 α-helix, before finally refolding into a β-strand that completes a three-stranded β-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. © 2012 Europhysics Letters Association.
Publication Title
EPL
Recommended Citation
Gaye, M.,
Hardwick, C.,
Kouza, M.,
&
Hansmann, U.
(2012).
Chameleonicity and folding of the C-fragment of TOP7.
EPL,
97(6).
http://doi.org/10.1209/0295-5075/97/68003
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/13127