Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 296, Issue 4, Pages 961-968Publisher
ACADEMIC PRESS LTD
DOI: 10.1006/jmbi.2000.3514
Keywords
amyloid; protein aggregation; fibril; protein design; binary patterning
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Recent experiments with combinatorial libraries of de novo proteins have demonstrated that sequences designed to contain polar and non-polar amino acid residues arranged in an alternating pattern form fibrillar structures resembling beta-amyloid. This finding prompted us to probe the distribution of alternating patterns in the sequences of natural proteins. Analysis of a database of 250,514 protein sequences (79,708,024 residues) for all possible binary patterns of polar and non-polar amino acid residues revealed that alternating patterns occur significantly less often than other patterns with similar compositions. The under-representation of alternating binary patterns in natural protein sequences, coupled with the observation that such patterns promote amyloid-like structures in de novo proteins, suggests that sequences of alternating polar and non-polar amino acids are inherently amyloidogenic and consequently have been disfavored by evolutionary selection. (C) 2000 Academic Press.
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