Proteins and related biomacromolecules are complex entities that exhibit fascinating behavior when interacting with other biomolecules. Light scattering provides a simple and effective means for characterizing the essential biophysical properties of proteins: molar mass, size, charge, interactions, conjugation and conformation.
- The DAWN HELEOS II and miniDAWN TREOS multi-angle light scattering detectors interfaces with any SEC system for determination of absolute molar mass via SEC-MALS and ASTRA software.
- Protein sizes are determined by adding a WyattQELS DLS module into the DAWN or miniDAWN.
- The DAWN also combines with the Calypso II composition-gradient system for the study of biomolecular interactions via CG-MALS and CALYPSO software.
- Rapid assessments of purity, aggregation and oligomerization may be made through size distributions via dynamic light scattering using a microwell-plate-based DynaPro Plate Reader II or a DynaPro NanoStar microcuvette-based instrument and the DYNAMICS software.
- Molecular charge of fragile biomolecules is determined by combining simultaneous electrophoretic mobility and size measurements in the Möbiuζ using DYNAMICS.