Reference : Lipid-Destabilising Properties Of A Peptide With Structural Plasticity
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Lipid-Destabilising Properties Of A Peptide With Structural Plasticity
Lorin, A. [> > > >]
Thomas, Annick [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Stroobant, V. [> > > >]
Brasseur, Robert mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Lins, Laurence mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Chemistry and Physics of Lipids
Yes (verified by ORBi)
[en] The Chameleon peptide (Cham) is a peptide designed from two regions of the GB1
protein, one folded as an alpha-helix and the other as a beta structure.
Depending on the environment, the Cham peptide adopts an alpha or a beta
conformation when inserted in different locations of GB1. This environment
dependence is also observed for tilted peptides. These short protein fragments,
able to destabilise organised system, are mainly folded in beta structure in
water and in alpha helix in a hydrophobic environment, like the lipid bilayer. In
this paper, we tested whether the Cham peptide can be qualified as a tilted
peptide. For this, we have compared the properties of Cham peptide
(hydrophobicity, destabilising properties, conformation) to those of tilted
peptides. The results suggest that Cham is a tilted peptide. Our study, together
the presence of tilted fragments in transconformational proteins, suggests a
relationship between tilted peptides and structural lability.
Researchers ; Professionals

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