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| Reference : Mechanochemical Study of Conformational Transitions in a Single Synthetic Peptide Chain |
| Scientific congresses and symposiums : Poster | |||
| Life sciences : Biochemistry, biophysics & molecular biology Physical, chemical, mathematical & earth Sciences : Multidisciplinary, general & others Physical, chemical, mathematical & earth Sciences : Physics Physical, chemical, mathematical & earth Sciences : Chemistry | |||
| http://hdl.handle.net/2268/126075 | |||
| Mechanochemical Study of Conformational Transitions in a Single Synthetic Peptide Chain | |
| English | |
Willet, Nicolas  [Université de Liège - ULg > Département de chimie (sciences) > Nano-chimie et systèmes moléculaires >] | |
| Hinterdorfer, Peter [Johannes Kepler University Linz > Biophysics Institute > > >] | |
| Lecommandoux, Sébastien [Université Bordeaux 1 > LCPO > > >] | |
| Duwez, Anne-Sophie [Université de Liège - ULg > Département de chimie (sciences) > Nano-chimie et systèmes moléculaires >] | |
| 5-Jun-2012 | |
| No | |
| International | |
| Gordon Research Conference: Biopolymers | |
| June 3-8, 2012 | |
| GRC | |
| Angel E. Garcia | |
| Enrique De La Cruz | |
| Newport | |
| Rhode Island, USA | |
| [en] AFM ; Single-molecule ; Peptide ; Folding ; Conformation | |
| [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 an alpha-helix and the reversibility of the phenomenon. | |
| NanoChem | |
| Researchers ; Students | |
| http://hdl.handle.net/2268/126075 |
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