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Published online before print May 28, 2004, 10.1110/ps.04663504
Protein Science (2004), 13:1939-1941. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates

Gian Gaetano Tartaglia, Andrea Cavalli, Riccardo Pellarin and Amedeo Caflisch

Department of Biochemistry, University of Zurich, CH-8057, Zurich, Switzerland

(RECEIVED February 2, 2004; FINAL REVISION March 18, 2004; ACCEPTED March 25, 2004)



Abstract

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.

Keywords: amyloid; prion; aggregation rate; Alzheimer; protein deposit; mutation

Reprint requests to: Amedeo Caflisch, Department of Biochemistry, University of Zurich, CH-8057, Zurich, Switzerland; e-mail: caflisch{at}bioc.unizh.ch; fax: +41-44-635-68-62.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04663504.

Supplemental material: see www.proteinscience.org


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