Thermal aggregation of patatin studied in situ

In this work dynamic light scattering was used to study the thermal aggrega tion of patatin in situ, to elucidate the physical aggregation mechanism of the protein and to be able to relate the aggregation behavior to its struc tural properties. The dependence of the aggregation rates on the temperatur e and the ionic strength suggested a mechanism of slow coagulation, being b oth diffusion and chemically limited. The aggregation rate dependence on th e protein concentration was in accordance with the mechanism proposed. The aggregation-rates as obtained at temperatures ranging from 40 to 65 degrees C correlated well with unfolding of the protein at a secondary level. Smal l-angle neutron scattering and dynamic light scattering results were in goo d accordance; they revealed that native patatin has a cylindrical shape wit h a diameter and length of 5 and 9.8 nm, respectively.