NR AXWC
AU Sekijima,M.; Motono,C.; Akiyama,Y.; Noguchi,T.
TI Free Energy Landscape Analysis of Prion Protein from Human, Bovine, Swine, Canine, Feline, Mouse, and Elk
QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Protein Misfolding P01.63
IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf
PT Konferenz-Poster
AB
Transmissible spongiform encephalopathies (TSEs) and prion disease are neurodegenerative disease caused by structure transformation of cellular prion (PrPc) to abnormal isoform (PrPsc). The most important theme in prion diseases is the conformational transition of PrPc to PrPsc. PrPc and PrPsc are isoforms with the same amino acid sequence, and, comparing between there secondary structures, PrPc has 42% of its residue folded in alpha-helices, 3% as ß-sheets, but PrPsc, in contrast, consists of 30% alpha-helices, 43% ß-sheets. However, the precise role of the normal PrPc, and chemical difference between PrPc and PrPsc, is still unknown. It appears that difference between them comes from only their conformational difference .
In this work, we used molecular dynamics (MD) simulation to evaluate molecular fluctuations. MD simulations are widely used for simulating the motions of molecules. Rapidly increasing computational power has made MD simulation a powerful tool for studying the structure and dynamics of biologically important molecules. To understand the thermodynamics and kinetics of protein folding, we developed a free energy landscape analysis system based on MD simulation. The calculation of free energy is of great importance for understanding the kinetics and the structural determinants of biomolecular processes, such as the folding and unfolding of proteins, ligand bindings to receptors and enzymes, and the transport of small molecules through channels.
We constructed free energy landscapes for seven species of prion protein. We will show the differences of free energy landscapes. Local minima analysis of them will be presented.
AD M. Sekijima, C. Motono, Y. Akiyama, T. Noguchi, National Institute of Advanced Industrial Science and Technology, Computational Biology Research Center, Japan
SP englisch
PO Schottland
EA pdf-Datei und Poster (Autorenliste auf M. Sekijima reduziert)