Phys. Rev. Lett. 77, 2324–2327 (1996)Entropic Barriers, Frustration, and Order: Basic Ingredients in Protein FoldingReceived 2 November 1995; published in the issue dated 9 September 1996 We consider the intrinsic entropy and energy barriers of cross-linking in a set of M monomers, plus minimal kinetic restrictions on the folding process of a proteinlike molecule. For a finite-size chain, there is an effective folding transition to an ordered structure. Without frustration, this state is reached in a time that scales as Mλ, with λ≃3. This scaling is limited by the amount of frustration which leads to the dynamical selectivity of proteins in a well defined range of temperatures, and M≲300 monomers. These predictions resemble generic properties of in vivo globular proteins. © 1996 The American Physical Society URL:
http://link.aps.org/doi/10.1103/PhysRevLett.77.2324
DOI:
10.1103/PhysRevLett.77.2324
PACS:
87.10.+e, 05.70.Fh, 64.60.Cn, 82.20.Db
|
|
About | Terms and Conditions | Subscriptions | Search | Help
Use of the American Physical Society websites and journals implies that the user has read and agrees to our Terms and Conditions and any applicable Subscription Agreement. Physical Review®, Physical Review Letters®, Reviews of Modern Physics®, and Physical Review Special Topics® are trademarks of the American Physical Society.