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The Key to Solving the Protein‐Folding Problem Lies in an Accurate Description of the Denatured State
Author(s) -
van Gunsteren Wilfred F.,
Bürgi Roland,
Peter Christine,
Daura Xavier
Publication year - 2001
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 - 10.1002/1521-3773(20010119)40:2<351::aid-anie351>3.0.co;2-6
Subject(s) - folding (dsp implementation) , protein folding , key (lock) , variety (cybernetics) , state (computer science) , process (computing) , computer science , chemistry , algorithm , artificial intelligence , engineering , mechanical engineering , biochemistry , computer security , operating system
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.