Interactions between lysozyme molecules under precrystallization conditions studied by light scattering - Skouri, M.; Munch, J.-P.; Lorber, B.; Giege, R.; Candau, S. (Elsevier)
Light scattering experiments were undertaken on lysozyme under various solvent conditions. When the protein is undersaturated, attractive interparticular interactions are detected. They are enhanced when the temperature is decreased, but are much weaker in NaCl solutions in which the protein crystallizes than in ammonium sulfate solutions in which it forms amorphous precipitates. When the protein in a NaCl solution is brought to supersaturation by a temperature decrease, light scattering measurements indicate the simultaneous presence of two scatter populations which can be assimilated to individual lysozyme molecules and to large particles. Kinetic experiments in which the temperature is quenched rapidly indicate that the apparent hydrodynamic radius of the large particles increases regularly with time up to a plateau value of about 2600 Å.
http://linkinghub.elsevier.com/retrieve/pii/0022-0248(92)90221-4
Keywords: V; TE-TZ; U