TY - JOUR
KW - Computer Simulation
KW - Protein Folding
KW - Thermodynamics
KW - Animals
KW - Humans
KW - Protein Conformation
KW - Proteins
KW - Alzheimer Disease
KW - Amino Acids
KW - Prions
AU - G. G. Tartaglia
AU - A. Cavalli
AU - R. Pellarin
AU - A. Caflisch
AB - <p>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.</p>
BT - Protein Science
C1 - 0058
DA - 2004 Jul
DO - 10.1110/ps.04663504
IS - 7
J2 - Protein Sci.
LA - eng
M3 - Research Article
N2 - <p>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.</p>
PY - 2004
SP - 1939
EP - 1941
T2 - Protein Science
TI - The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
VL - 13
SN - 0961-8368
ER -