Reference : Mechanochemistry of a single polypeptide molecule: Study of force-induced conformatio...
Scientific congresses and symposiums : Unpublished conference
Life sciences : Biochemistry, biophysics & molecular biology
Physical, chemical, mathematical & earth Sciences : Multidisciplinary, general & others
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/107215
Mechanochemistry of a single polypeptide molecule: Study of force-induced conformational transitions
English
Willet, Nicolas mailto [University of Liège - ULg > Department of Chemistry > Nanochemistry and Molecular Systems > >]
Hinterdorfer, Peter [Johannes Kepler University of Linz > > Biophysics Institute > >]
Lecommandoux, Sébastien [University Bordeaux 1 > > Laboratoire de Chimie des Polymères Organiques (LCPO) > >]
Duwez, Anne-Sophie mailto [University of Liège - ULg > Department of Liège > Nanochemistry and Molecular Systems > >]
Aug-2011
No
No
International
AFM BioMed Conference
23-27/08/2011
Paris
France
[en] The aim of this study is to investigate the mechanochemical behavior of homopolypeptides able to change their conformation is a stimuli-responsive way. The peptidic secondary structures were studied in detail by atomic force microscopy (AFM) at the single-molecule level.
Synthetic copolymers containing a polypeptide block were prepared by N-carboxyanhydride amino acid ring-opening polymerization. The polymer chains were grafted as a dilute brush onto gold surfaces via disulfide end-groups. Their mechanochemical behavior was then studied by AFM single-molecule force spectroscopy (SMFS). The investigated polypeptide blocks were based on poly(L-glutamic acid), which undergoes a transition from alpha-helix to random coil. This can be induced by external stimuli (pH, ionic strength, temperature) or simply by applying a force.
We were able to study the mechanically driven unfolding of the peptide by stretching-release cycles of the biomacromolecule. Stretching the helical peptide resulted in original features in the force-distance traces. Plateaus that are specific for the helical conformation were detected, quantified and discussed. Pulling-relaxing SMFS experiments eventually led to a better understanding of the force induced unfolding of a alpha-helix and the reversibility of the phenomenon.
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http://hdl.handle.net/2268/107215
http://afmbiomed.org/2011-paris.aspx

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