Exploring amyloid formation by a de novo design.
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ABSTRACT:
SUBMITTER: Kammerer RA
PROVIDER: S-EPMC384765 | biostudies-literature | 2004 Mar
REPOSITORIES: biostudies-literature
Publications
Exploring amyloid formation by a de novo design.
Kammerer Richard A RA Kostrewa Dirk D Zurdo Jesús J Detken Andreas A García-Echeverría Carlos C Green Janelle D JD Müller Shirley A SA Meier Beat H BH Winkler Fritz K FK Dobson Christopher M CM Steinmetz Michel O MO
Proceedings of the National Academy of Sciences of the United States of America 20040226 13
Protein deposition as amyloid fibrils underlies many debilitating human disorders. The complexity and size of disease-related polypeptides, however, often hinders a detailed rational approach to study effects that contribute to the process of amyloid formation. We report here a simplified peptide sequence successfully designed de novo to fold into a coiled-coil conformation under ambient conditions but to transform into amyloid fibrils at elevated temperatures. We have determined the crystal str ...[more]
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