Publikation: The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State
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2001
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Angewandte Chemie International Edition. 2001, 40(2), pp. 351-355. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/1521-3773(20010119)40:2<351::AID-ANIE351>3.0.CO;2-6
Zusammenfassung
Accurate simulation at the atomic level of the folding process of a variety of peptides into different native folds (see picture) can be achieved with a general purpose force field and Newton's equations of motion. The key to understanding this peptide folding lies in the unexpectedly small size of the denatured state and an accurate description thereof.
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540 Chemie
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VAN GUNSTEREN, Wilfred F., Roland BÜRGI, Christine PETER, Xavier DAURA, 2001. The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State. In: Angewandte Chemie International Edition. 2001, 40(2), pp. 351-355. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/1521-3773(20010119)40:2<351::AID-ANIE351>3.0.CO;2-6BibTex
@article{vanGunsteren2001-01-19Solvi-40150, year={2001}, doi={10.1002/1521-3773(20010119)40:2<351::AID-ANIE351>3.0.CO;2-6}, title={The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State}, number={2}, volume={40}, issn={1433-7851}, journal={Angewandte Chemie International Edition}, pages={351--355}, author={van Gunsteren, Wilfred F. and Bürgi, Roland and Peter, Christine and Daura, Xavier} }
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