| Abstract: | The tertiary and quaternary structure of α-crystallin is still a matter of controversy. We have characterized the native α-crystallin quaternary structure by isolating it at the in vivo temperature and solvent conditions. It can be represented by a distribution of expanded particles with a weight average molar mass of 550 000 g/mol. On decreasing (to 4°C) or increasing (up to 50°C) the temperature, the size distribution increases to larger particles. Only at lower temperatures (4°C), a stable population of particles is obtained with weight average molar mass of 700 000 g/mol. In all conditions, α-crystallin behaves as a very expanded particle with a maximum hydrodynamic volume of 3.15 ml/g. The transitions in quaternary structure are rather slow: it takes several hours to evolve from a population of aggregates, characteristic for given solvent conditions, to another distribution in size and quaternary structure on changing the environment. The quaternary structure of α-crystallin is an uncharacteristic parameter of the particle: a broad distribution of values can be obtained on changing the environment. Any realistic model should include this property. Our studies favor an open loose structure, where peptides can be added or removed without drastic changes of secondary and tertiary structure of the peptides. |
