We present a numerical study of a new protein model. This off-lattice model takes into
account both the hydrogen bonds and the amino-acid interactions. It reproduces the folding of
a small protein (peptide): morphological analysis of the conformations at low temperature
shows two well-known substructures α-helix and β-sheet depending on the chosen sequence.
The folding pathway in the scope of this model is studied through a free-energy analysis.
We then study the aggregation of proteins. Proteins in the aggregate are mainly bound via
hydrogen bonds. Performing a free-energy analysis we show that the addition of a peptide to
such an aggregate is not favourable. We qualitatively reproduce the abnormal aggregation of
proteins in prion diseases
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