Simulation of Top7-CFr: a transient helix extension guides folding

Mohanty, S.; Meinke, J.; Zimmermann, O.; Hansmann, U. H. E.

doi:10.1073/pnas.0708411105

Journal Article

Simulation of Top7-CFr: a transient helix extension guides folding

Mohanty, S.FZJ* ; Meinke, J.FZJ* ; Zimmermann, O.FZJ* ; Hansmann, U. H. E.FZJ*

2008
Academy Washington, DC

Proceedings of the National Academy of Sciences of the United States of America 105, 8004 - 8007 (2008) [10.1073/pnas.0708411105]

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Please use a persistent id in citations: doi:10.1073/pnas.0708411105

Abstract: Protein structures often feature beta-sheets in which adjacent beta-strands have large sequence separation. How the folding process orchestrates the formation and correct arrangement of these strands is not comprehensively understood. Particularly challenging are proteins in which beta-strands at the N and C termini are neighbors in a beta-sheet. The N-terminal beta-strand is synthesized early on, but it can not bind to the C terminus before the chain is fully synthesized. During this time, there is a danger that the beta-strand at the N terminus interacts with nearby molecules, leading to potentially harmful aggregates of incompletely folded proteins. Simulations of the C-terminal fragment of Top7 show that this risk of misfolding and aggregation can be avoided by a "caching" mechanism that relies on the "chameleon" behavior of certain segments.

Keyword(s): Computer Simulation (MeSH) ; Peptide Fragments: chemistry (MeSH) ; Protein Folding (MeSH) ; Protein Structure, Secondary (MeSH) ; Proteins: chemistry (MeSH) ; Proteins: metabolism (MeSH) ; Temperature (MeSH) ; Thermodynamics (MeSH) ; Peptide Fragments ; Proteins ; J ; protein folding (auto) ; all-atom simulation (auto) ; folding mechanism (auto) ; chameleon segment (auto) ; nonnative intermediates (auto)