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Title

 

 

 

 

 

Analysis of protein chameleon sequence characteristics

 

Authors

 

Amine Ghozlane1, Agnel Praveen Joseph1,2, Aurelie Bornot1, Alexandre G. de Brevern1*

 

Affiliation

 

 

1Equipe de Bioinformatique Génomique et Moléculaire (EBGM), INSERM UMR-S 726, DSIMB, Université Paris Diderot- Paris 7, Institut National de Transfusion Sanguine (INTS), 6, rue Alexandre Cabanel, 75739 Paris cedex 15, France ; 2Molecular Biophysics Unit, Indian Institute of Science Bangalore 560 012, India

 

Email

 

alexandre.debrevern@univ-paris-diderot.fr

Article Type

 

Hypothesis

Date

 

received November 10, 2008; revised January 06, 2009; accepted January 14, 2009; published May 04, 2009
 

Abstract

Conversion of local structural state of a protein from an α-helix to a β-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 α -helices, β-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 prefer coil state over to the regular secondary structures. About half of them show preference for both α -helix and β-sheet conformations and either of these two states is favored by the rest.

 

Keywords

chameleon sequence, structural characteristics, secondary structures

 

Citation

Ghozlane et al, Bioinformation 3(9): 367-369 (2009)
 

Edited by

B. Offmann

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

License

 

 

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.