Volume 97, Number 6, March 2012
|Number of page(s)||6|
|Section||Interdisciplinary Physics and Related Areas of Science and Technology|
|Published online||15 March 2012|
Chameleonicity and folding of the C-fragment of TOP7
Wayne County Community College District - Detroit, MI 48226, USA
2 Department of Physics, Michigan Technological University - Houghton, MI 49931, USA
3 Department of Chemistry & Biochemistry, University of Oklahoma - Norman, OK 73019, USA
Accepted: 14 February 2012
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.
PACS: 87.15.Cc – Folding: thermodynamics, statistical mechanics, models, and pathways / 87.15.hp – Conformational changes / 87.15.hm – Folding dynamics
© EPLA, 2012
Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.
Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.
Initial download of the metrics may take a while.