The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
- 1 July 2004
- journal article
- Published by Wiley in Protein Science
- Vol. 13 (7), 1939-1941
- https://doi.org/10.1110/ps.04663504
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
This publication has 15 references indexed in Scilit:
- Rationalization of the effects of mutations on peptide andprotein aggregation ratesNature, 2003
- Chain Length Dependence of Apomyoglobin Folding: Structural Evolution from Misfolded Sheets to Native HelicesBiochemistry, 2003
- The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35Proceedings of the National Academy of Sciences, 2003
- Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseasesProceedings of the National Academy of Sciences, 2002
- A possible role for π‐stacking in the self‐assembly of amyloid fibrilsThe FASEB Journal, 2002
- Evaluation of a fast implicit solvent model for molecular dynamics simulationsProteins-Structure Function and Bioinformatics, 2001
- Protein misfolding, evolution and diseaseTrends in Biochemical Sciences, 1999
- The alternative conformations of amyloidogenic proteins and their multi-step assembly pathwaysCurrent Opinion in Structural Biology, 1998
- Hydrophobicity regainedProtein Science, 1997
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983