While there are many ways to determine the molar masses, or molecular weights of macromolecules such as proteins, biopolymers and synthetic polymers, only Multi-Angle static Light Scattering (MALS) determines absolute molecular weights in solution, rapidly and effectively.

MALS combines the precise measurements of light scattering intensity and concentrations for a rigorous, first-principles calculation of solution-property molecular weights—making no assumptions of conformation or shape, and no perturbations to the sample.

Molar Mass By On-line (fractionated) Multi-Angle Light Scattering (SEC-MALS)

MALS detectors are most commonly intergrated with a separation technique such as size exclusion chromatography (SEC-MALS) Incorporation of independent, absolute MALS analysis eliminates reliance on unreliable column calibration, retention time and models of hydrodynamic size vs. molar mass in order to provide accurate molar mass distributions across the chromatogram.

Important Applications of SEC-MALS

• Molar mass distribution of heterogeneous samples such as carbohydrates or synthetic polymers
• Accurate aggregation and oligomeric states of proteins, peptides and virus-like particles
• Stoichiometry of tightly bound protein heterocomplexes.

Molar Mass via Dynamic Light Scattering (DLS)

Strictly speaking, Dynamic Light Scattering (DLS) measures the diffusion constant of particles in solution and cannot determine molar mass directly and rigorously. DLS analysis estimates molar mass in the DYNAMICS software by converting the diffusion constant to an effective size and invoking models that assume relationships between size and mass.