Light scattering studies on Ficoll PM70 solutions reveal two distinct diffusive modes.

Ficoll PM70 is an important branched polysaccharide polymer with a variety of applications in biology and biophysics. The accepted picture for the aqueous solutions of this polymer is that of a polydisperse nearly spherical suspension with a molecular weight of 70.0 kDa and a hydrodynamic radius α=(4.

The eye lens chaperone alpha-crystallin forms defined globular assemblies.

Alpha-crystallins are molecular chaperones that protect vertebrate eye lens proteins from detrimental protein aggregation. alphaB-Crystallin, 1 of the 2 alpha-crystallin isoforms, is also associated with myopathies and neuropathological diseases. Despite the importance of alpha-crystallins in protein homeostasis, only little is known about their quaternary structures because of their seemingly polydisperse nature.

Lysozyme aggregation studied by light scattering. II. Variations of protein concentration.

Static and dynamic light scattering have been employed to investigate the behaviour of nucleating lysozyme solutions in the range between 0.34 and 3.08 mM.

Lysozyme aggregation studied by light scattering. I. Influence of concentration and nature of electrolytes.

Static and dynamic light scattering have been employed to investigate the behaviour of lysozyme solutions when varying the concentration of (NH(4))(2)SO(4) and NaCl for screening the repulsive forces between the monomers. At the initial aggregation stages clusters, which can be classified as mass-fractals undergoing diffusion limited-like aggregation, coexist with monomers or small lysozyme oligomers. The kinetics of fractal growth deliver observables that exhibit distinct tendencies when examined as a function of the concentration and nature of the electrolyte.

Comparison of two different lysozyme types under native and crystallization conditions using two-dimensional NMR and dynamic light scattering.

In order to elucidate differences observed in the aggregation kinetics of hen-egg white lysozyme under crystallization conditions we have undertaken a comparative study of the enzyme marketed by Seikagaku and Sigma companies. When the crystallization of the two lysozyme preparations is followed by time-resolved dynamic light scattering, the structural differences are also observed under native conditions in the early nucleation kinetics. The differences are manifested in the formation rates of macroscopic crystals, but do not influence the morphology of the typical tetragonal lysozyme crystal.