Fast folding of a helical protein initiated by the collision of unstructured chains

W. Kevin Meisner, Tobin R. Sosnick

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

To examine whether helix formation necessarily precedes chain collision, we have measured the folding of a fully helical coiled coil that has been specially engineered to have negligible intrinsic helical propensity but high overall stability. The folding rate approaches the diffusion-limited value and is much faster than possible if folding is contingent on precollision helix formation. Therefore, the collision of two unstructured chains is the initial step of the dominant kinetic pathway, whereas helicity exerts its influence only at a later step. Folding from an unstructured encounter complex may be efficient and robust, which has implications for any biological process that couples folding to binding.

Original languageEnglish (US)
Pages (from-to)13478-13482
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number37
DOIs
StatePublished - Sep 14 2004

Keywords

  • Binding
  • Diffusion
  • Helix formation
  • Natively unfolded
  • Transition state

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