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Peptide Folding: When Simulation Meets Experiment
Author(s) -
Daura Xavier,
Gademann Karl,
Jaun Bernhard,
Seebach Dieter,
van Gunsteren Wilfred F.,
Mark Alan E.
Publication year - 1999
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19990115)38:1/2<236::aid-anie236>3.0.co;2-m
Subject(s) - folding (dsp implementation) , computer science , engineering , mechanical engineering
Accurate reproduction of the mechanism of peptide folding in solution and conformational preferences as a function of amino acid sequence is possible with atomic level dynamics simulations. For example, the simulations correctly predict a left‐handed 3 1 ‐helical fold for the β ‐heptapeptide 1 (the molecular model is shown in the picture) and a right‐handed helical fold for the β ‐hexapeptide 2 , as was confirmed by NMR spectroscopy.