%0 Journal Article
%A Mohanty, S.
%A Meinke, J.
%A Zimmermann, O.
%A Hansmann, U. H. E.
%T Simulation of Top7-CFr: a transient helix extension guides folding
%J Proceedings of the National Academy of Sciences of the United States of America
%V 105
%@ 0027-8424
%C Washington, DC
%I Academy
%M PreJuSER-519
%P 8004 - 8007
%D 2008
%Z Record converted from VDB: 12.11.2012
%X 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.
%K Computer Simulation
%K Peptide Fragments: chemistry
%K Protein Folding
%K Protein Structure, Secondary
%K Proteins: chemistry
%K Proteins: metabolism
%K Temperature
%K Thermodynamics
%K Peptide Fragments (NLM Chemicals)
%K Proteins (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:18408166
%2 pmc:PMC2786944
%U <Go to ISI:>//WOS:000256781800020
%R 10.1073/pnas.0708411105
%U https://juser.fz-juelich.de/record/519