NR ARMP
AU Tartaglia,G.G.; Cavalli,A.; Pellarin,R.; Caflisch,A.
TI The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
QU Protein Science 2004 Jul; 13(7): 1939-41
IA http://www.proteinscience.org/cgi/content/full/13/7/1939
PT journal article
AB The mechanisms by which peptides and proteins form ordered aggregates are not well understood. Here we focus on the physicochemical properties of amino acids that favor ordered aggregation and suggest a parameter-free model that is able to predict the change of aggregation rates over a large set of natural sequences. Furthermore, the results of the parameter-free model correlate well with the aggregation propensities of a set of peptides designed by computer simulations.
MH Alzheimer Disease/metabolism; Amino Acids/*chemistry/metabolism; Animals; *Computer Simulation; Humans; Prions/chemistry/metabolism; Protein Conformation; *Protein Folding; Proteins/*chemistry/metabolism; Research Support, Non-U.S. Gov't; Thermodynamics
AD Department of Biochemistry, University of Zürich, CH-8057, Zürich, Switzerland.
SP englisch
PO USA