The Fast and the Slow: Folding and Trapping of λ6–85
Citations Over TimeTop 14% of 2011 papers
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.
Related Papers
- → Microsecond folding experiments and simulations: a match is made(2013)54 cited
- → Probing emission of a DNA-stabilized silver nanocluster from the sub-nanosecond to millisecond timescale in a single measurement(2022)20 cited
- → An on/off resonance rotating frame relaxation experiment to monitor millisecond to microsecond timescale dynamics(2004)10 cited
- → Faculty Opinions recommendation of NMR Method for Characterizing Microsecond-to-Millisecond Chemical Exchanges Utilizing Differential Multiple-Quantum Relaxation in High Molecular Weight Proteins.(2016)