Malvern Instruments systems measure fundamental parameters known to affect dispersion stability.
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I want to characterize Proteins

Measurements of proteins by light scattering and SEC can provide a great deal of information including absolute molecular weight, absolute size, oligomerisation state, aggregate formation and sample polydispersity, melting point, conjugate composition and second virial coefficient.

I want to measure:

 
  
Protein Hydrodynamic size
Size relates directly to protein conformation and, thus, its function. The size and quality of a protein sample and its likely activity can be assessed through DLS measurements.
 
Protein Molecular Weight
The intensity of scattered light is proportional to a molecule's molecular weight. The absolute molecular weight of a pure protein can be measured using light scattering techniques
 
Proteins using Size-Exclusion Chromatography
Adding light scattering to the end of a size exclusion chromatography system allows absolute measurement of protein size independently from column calibration. The regular structure of proteins means the size can be related to their molecular weight.
 
Protein melting point
The temperature at which a protein breaks down and loses its structure is its melting point. Performing temperature dependent size measurements allows the melting point of a protein to be estimated.
 
Protein crystallization
Crystallization likelihood can be assessed by monitoring the polydispersity (size distribution width) of a sample. A sample with low polydispersity will have a greater chance of crystallizing.
 
Aggregate formation
Protein aggregation is a key step in the loss of its activity. Light scattering is disproportionally sensitive to larger molecules making it particularly sensitive to the early stages of aggregate formation.


 
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