Analysis of protein chameleon sequence characteristics. - Inserm - Institut national de la santé et de la recherche médicale Access content directly
Journal Articles Bioinformation Year : 2009

Analysis of protein chameleon sequence characteristics.


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.
Fichier principal
Vignette du fichier
R1_Ghozlane_Jospeh_Bornot_de_Brevern_manuscript.pdf (343.25 Ko) Télécharger le fichier
Origin Files produced by the author(s)

Dates and versions

inserm-00353122 , version 1 (24-09-2009)


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


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


174 View
146 Download



Gmail Mastodon Facebook X LinkedIn More