In analytical ultracentrifugation (AUC), molecules are characterized directly in solution, often under biologically relevant conditions. In contrast to many other methods, there are no complications caused by interactions with matrices or surfaces. Also, no immobilization or labeling is necessary for the analysis. Analytical ultracentrifugation is considered to be one of the most accurate methods for determination of molar mass of the molecule. Since it is a first-principle method, no calibration is required to determine the mass. AUC is a non-destructive technique which is applicable to particles with molar masses ranging from several hundreds of Da (small peptides) to hundreds of MDa (viruses).
Beckman Coulter ProteomeLab XL-I - The instrument is equipped with absorbance optics (wavelength range 190 – 800 nm) and interference optics and can be used for both sedimentation velocity and sedimentation equilibrium experiments. Analytical ultracentrifugation has a broad applicability in science including determination of sample homogeneity, oligomeric state of proteins (or molecular weight, respectively) and can be used to assess aggregation and to study biomolecular interactions of self- and hetero-association systems (determination of stoichiometry and affinity, affinity can be determined usually in the range of 104-107 M-1).
These requirements depend on the nature of experiments and a particular system. Details of the experiment should be further discussed.