Contact order revisited: Influence of protein size on the folding rate

Dmitry N. Ivankov, Sergiy O. Garbuzynskiy, Eric Alm, Kevin W. Plaxco, David Baker, Alexei V. Finkelstein

Research output: Contribution to journalArticlepeer-review

312 Citations (Scopus)

Abstract

Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L2/3, and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO × L, is able to predict rather accurately folding rates for both two-state and multistate folding proteins, as well as short peptides, and that this Abs_CO scales with the protein chain length as L0.70±0.07 for the totality of studied single-domain proteins and peptides.

Original languageEnglish
Pages (from-to)2057-2062
Number of pages6
JournalProtein Science
Volume12
Issue number9
DOIs
Publication statusPublished - 1 Sep 2003
Externally publishedYes

Keywords

  • Contact order
  • Multistate kinetics
  • Protein folding kinetics
  • Protein size
  • Protein topology
  • Rate of folding
  • Two-state kinetics

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