Open AccessIs there a single pathway for the folding of a polypeptide chain?
Author(s) -
Stephen C. Harrison,
Richard Durbin
Publication year - 1985
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.12.4028
Subject(s) - folding (dsp implementation) , protein folding , polypeptide chain , computational biology , chain (unit) , chemistry , amino acid , computer science , biology , biochemistry , physics , astronomy , electrical engineering , engineering
We argue that folding of the compact domains of proteins can occur with adequate rapidity in the absence of a unique directed mechanism, provided that native-like local structure dominates the folding process. We further suggest that the evolution of amino acid sequences should favor multiple paths to the folded state. Existing physicochemical and mutational data are not inconsistent with a many-pathway model. The analogy of a jigsaw puzzle, with multiple routes to a unique solution, appears to be particularly apt.