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Analysis of protein chameleon sequence characteristics.

Abstract : Conversion of local structural state of a protein from an alpha-helix to a beta-strand is usually associated with a major change in the tertiary structure. Similar changes were observed during the self assembly of amyloidogenic proteins to form fibrils, which are implicated in severe diseases conditions, e.g., Alzheimer disease. Studies have emphasized that certain protein sequence fragments known as chameleon sequences do not have a strong preference for either helical or the extended conformations. Surprisingly, the information on the local sequence neighborhood can be used to predict their secondary at a high accuracy level. Here we report a large scale-analysis of chameleon sequences to estimate their propensities to be associated with different local structural states such as alpha -helices, beta-strands and coils. With the help of the propensity information derived from the amino acid composition, we underline their complexity, as more than one quarter of them prefers coil state over to the regular secondary structures. About half of them show preference for both alpha-helix and beta-sheet conformations and either of these two states is favored by the rest.
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Contributor : Alexandre G. de Brevern Connect in order to contact the contributor
Submitted on : Thursday, September 24, 2009 - 10:01:37 AM
Last modification on : Saturday, June 25, 2022 - 8:48:37 PM
Long-term archiving on: : Tuesday, June 8, 2010 - 6:05:08 PM


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  • HAL Id : inserm-00353122, version 1
  • PUBMED : 19759809



Amine Ghozlane, Agnel Joseph, Aurélie Bornot, Alexandre de Brevern. Analysis of protein chameleon sequence characteristics.. Bioinformation, Biomedical Informatics Publishing Group, 2009, 3 (9), pp.367-9. ⟨inserm-00353122⟩



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