TY  - JOUR
AU  - Meinke, J.
AU  - Hansmann, U.
TI  - Aggregation of Beta-Amyloid Fragments
JO  - The journal of chemical physics
VL  - 126
SN  - 0021-9606
CY  - Melville, NY
PB  - American Institute of Physics
M1  - PreJuSER-55426
SP  - 014706
PY  - 2007
N1  - Record converted from VDB: 12.11.2012
AB  - The authors study the folding and aggregation of six chains of the beta-amyloid fragment 16-22 using Monte Carlo simulations. While the isolated fragment prefers a helical form at room temperature, in the system of six interacting fragments one observes both parallel and antiparallel beta sheets below a crossover temperature T(x) approximately equal to 420 K. The antiparallel sheets have lower energy and are therefore more stable. Above the nucleation temperature the aggregate quickly dissolves into widely separated, weakly interacting chains.
KW  - Amyloid beta-Peptides: chemistry
KW  - Amyloid beta-Peptides: ultrastructure
KW  - Binding Sites
KW  - Computer Simulation
KW  - Dimerization
KW  - Models, Chemical
KW  - Models, Molecular
KW  - Monte Carlo Method
KW  - Multiprotein Complexes: chemistry
KW  - Multiprotein Complexes: ultrastructure
KW  - Peptide Fragments: chemistry
KW  - Peptide Fragments: ultrastructure
KW  - Protein Binding
KW  - Protein Conformation
KW  - Protein Folding
KW  - Temperature
KW  - Amyloid beta-Peptides (NLM Chemicals)
KW  - Multiprotein Complexes (NLM Chemicals)
KW  - Peptide Fragments (NLM Chemicals)
KW  - amyloid beta-protein (16-22) (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:17212510
UR  - <Go to ISI:>//WOS:000243380000031
DO  - DOI:10.1063/1.2423013
UR  - https://juser.fz-juelich.de/record/55426
ER  -