Measurements of proteins by light scattering can provide a great deal of information including folded size and oligomerisation state, aggregate formation and sample polydispersity, melting point and molecular weight.
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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.
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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
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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.
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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.
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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.
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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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