Abstract
Nanosecond time-resolved optical rotatory dispersion (TRORD) techniques are coupled with laser temperature-jump (T-jump) triggering in an instrument that measures ultrafast protein folding-unfolding dynamics with high specificity to secondary structure. Far-ultraviolet (UV) ORD can be measured with this instrument over a wide wavelength range at times as early as 35 ns after a 3 ns laser T-jump pulse. The fundamental of a Nd:YAG laser is passed through a D2-filled Raman shifter to generate a pulse of 1.5μm infrared (IR) light that is efficiently absorbed by water. The resulting T-jump is stable for at least 1 ms before decaying back to the starting temperature with a time constant of ∼30ms. The ability to measure entire TRORD band shapes during this temporal window makes it possible to distinguish between changes in the signal due to a genuine unfolding or refolding process and changes due to artifacts. The technique, applicable to a wide variety of proteins, is demonstrated here in submillisecond unfolding studies of RNAse A and cytochrome c.
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