This research was supported by the NSF (Postdoctoral Fellowship in Biological Sciences, J.M.B.), the Hughes Hall Fellowship, the University of Cambridge (J.M.B.), and the Medical Research Council (J.G.). We are grateful to Dr. P. Tessier and Dr. S. Lindquist for providing fluorescence intensities, and to Dr. C. M. Dobson and Dr. S. Radford for critical reading of the manuscript.
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Zuschrift
Identification of Aggregation-Prone Elements by Using Interaction-Energy Matrices†
Article first published online: 8 AUG 2008
DOI: 10.1002/ange.200802345
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Bui, Jennifer M., Cavalli, A. and Gsponer, J. (2008), Identification of Aggregation-Prone Elements by Using Interaction-Energy Matrices. Angew. Chem., 120: 7377–7379. doi: 10.1002/ange.200802345
- †
Publication History
- Issue published online: 3 SEP 2008
- Article first published online: 8 AUG 2008
- Manuscript Received: 20 MAY 2008
Funded by
- Medical Research Council
Keywords:
- Aggregation;
- Coaggregation;
- Computerchemie;
- Proteine;
- Wechselwirkungsenergien
Zahlreiche Krankheitsbilder werden mit der Umwandlung löslicher Proteine in Amyloidaggregate in Verbindung gebracht. Die Peptidwechselwirkungsmatrix-Analyse, ein neues First-Principles-Rechenverfahren, identifiziert zur Aggregation neigende Peptide, die antiparallele (siehe Bild) oder parallele β-Faltblattbereiche bilden, und gibt Auskunft über die Wahrscheinlichkeit einer (Co)Aggregation.