Simulation of Top7-CFr: A transient helix extension guides folding
Document Type
Article
Publication Date
6-10-2008
Abstract
Protein structures often feature β-sheets in which adjacent β-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 β-strands at the N and C termini are neighbors in a β-sheet. The N-terminal β-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 β-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. © 2008 by The National Academy of Sciences of the USA.
Publication Title
Proceedings of the National Academy of Sciences of the United States of America
Recommended Citation
Mohanty, S.,
Meinke, J.,
Zimmermann, O.,
&
Hansmann, U.
(2008).
Simulation of Top7-CFr: A transient helix extension guides folding.
Proceedings of the National Academy of Sciences of the United States of America,
105(23), 8004-8007.
http://doi.org/10.1073/pnas.0708411105
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/9033