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| Reference : Mechanochemistry of a single polypeptide molecule: Study of force-induced conformational... |
| Scientific congresses and symposiums : Unpublished conference | |||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  [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 [University of Liège - ULg > Department of Liège > Nanochemistry and Molecular Systems > >] | |
| Aug-2011 | |
| 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. | |
| Researchers ; Professionals ; Students | |
| http://hdl.handle.net/2268/107215 | |
| http://afmbiomed.org/2011-paris.aspx |
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