Sibille L, Pusey M L
Marshall Space Flight Center, Biophysics, Huntsville, AL 35812, USA.
Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):396-7. doi: 10.1107/S0907444993013447.
This laboratory has explored the potential of a combination of three analytical techniques to study the nucleation of chicken egg-white lysozyme. Collisional quenching of the fluorescent molecule SPQ [6-methoxy-N-(3-sulfopropyl)quinolinium] by chloride ions was used to determine the binding of the crystallizing agent to the protein at equilibrium and kinetically. Calorimetric measurements show that this binding generates an exothermic peak larger than the energy released during the early stages of nucleation. Light scattering intensity measurements were used to follow the aggregation kinetics.