The fast and the slow: Folding and trapping of λ 6-85

Maxim B. Prigozhin, Martin Gruebele

Research output: Contribution to journalArticlepeer-review


Molecular dynamics simulations combining many microsecond trajectories have recently predicted that a very fast folding protein like lambda repressor fragment λ 6-85 D14A could have a slow millisecond kinetic phase. We investigated this possibility by detecting temperature-jump relaxation to 5 ms. While λ 6-85 D14A has no significant slow phase, two even more stable mutants do. A slow phase of λ 6-85 D14A does appear in mild denaturant. The experimental data and computational modeling together suggest the following hypothesis: λ 6-85 takes only microseconds to reach its native state from an extensively unfolded state, while the latter takes milliseconds to reach compact β-rich traps. λ 6-85 is not only thermodynamically but also kinetically protected from reaching such "intramolecular amyloids" while folding.

Original languageEnglish (US)
Pages (from-to)19338-19341
Number of pages4
JournalJournal of the American Chemical Society
Issue number48
StatePublished - Dec 7 2011

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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