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Updated: Jun 28, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
Caching of a chameleon segment facilitates folding of a protein with end-to-end beta-sheet
Sandipan Mohanty1, Ulrich H E Hansmann
1John von Neumann-Institut für Computing, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Abstract:
We report results from all-atom simulations of a 49-residue C-terminal fragment of TOP7 in implicit solvent. Using parallel tempering simulations with high statistics, we probe the thermodynamic properties of the protein over a large range of temperatures and evaluate its free energy landscape at room temperature. Our results confirm that the protein folds by a caching mechanism that relies on a chameleon segment. This mechanism differs from the one seen in high-temperature unfolding simulations. Finally, we discuss a possible mechanism for dimerization of the protein.
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