Abstract
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 language | English (US) |
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Pages (from-to) | 19338-19341 |
Number of pages | 4 |
Journal | Journal of the American Chemical Society |
Volume | 133 |
Issue number | 48 |
DOIs | |
State | Published - Dec 7 2011 |
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry