L. Sibille et Ml. Pusey, INVESTIGATION OF NUCLEATING LYSOZYME SOLUTIONS, Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 396-397
This laboratory has explored the potential of a combination of three a
nalytical techniques to study the nucleation of chicken egg-white lyso
zyme. 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 a
nd kinetically. Calorimetric measurements show that this binding gener
ates an exothermic peak larger than the energy released during the ear
ly stages of nucleation. Light scattering intensity measurements were
used to follow the aggregation kinetics.