TY  - JOUR
AU  - Mohanty, S.
AU  - Meinke, J.
AU  - Zimmermann, O.
AU  - Hansmann, U. H. E.
TI  - Simulation of Top7-CFr: a transient helix extension guides folding
JO  - Proceedings of the National Academy of Sciences of the United States of America
VL  - 105
SN  - 0027-8424
CY  - Washington, DC
PB  - Academy
M1  - PreJuSER-519
SP  - 8004 - 8007
PY  - 2008
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Computer Simulation
KW  - Peptide Fragments: chemistry
KW  - Protein Folding
KW  - Protein Structure, Secondary
KW  - Proteins: chemistry
KW  - Proteins: metabolism
KW  - Temperature
KW  - Thermodynamics
KW  - Peptide Fragments (NLM Chemicals)
KW  - Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:18408166
C2  - pmc:PMC2786944
UR  - <Go to ISI:>//WOS:000256781800020
DO  - DOI:10.1073/pnas.0708411105
UR  - https://juser.fz-juelich.de/record/519
ER  -