PMC:2724026 / 33200-33860 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/2724026","sourcedb":"PMC","sourceid":"2724026","source_url":"https://www.ncbi.nlm.nih.gov/pmc/2724026","text":"For WT and mutants, refolding and unfolding were monitored by changes in fluorescence, using an Applied Photophysics SX.18MV stopped-flow fluorimeter. An excitation wavelength of 280 nm was used with a 320 nm cut-off filter; the final concentration of protein was 1–2 μM. WT kinetics were also monitored by CD using an Applied Photophysics Π⁎-180 instrument, with a final maximum concentration of protein of 5 μM. In both cases, the stopped-flow apparatus was maintained at 25(± 0.1) °C. Data collected from 8–12 experiments were averaged and traces were fit to a single-exponential function. Kinetic traces were analysed using Kaleidagraph (Synergy Software).","tracks":[]}