nanoDSF (Nano Differential Scanning Fluorimetry) is used on our platform for thermostability assessment of proteins. This label-free technique measures melting temperatures by monitoring intrinsic fluorescence changes during thermal unfolding.

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How It Works

Upon increasing temperature, the hydrophobic core of proteins unfolds, exposing aromatic amino acids (tryptophan and tyrosine) that produce fluorescent signals. The fluorescence intensity changes over time as the protein unfolds, and we take the first derivative of this signal to create a peak from which we can compute the melting temperature (Tm).

Important Caveat: This technique works best for proteins with a hydrophobic core containing aromatic amino acids. Some de novo mini binders might not have sufficient aromatic amino acids to produce a strong fluorescent signal.

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Temperature Range

We can measure thermostability from room temperature to 95°C, providing comprehensive thermal profiles for protein characterization.

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Protein Types

nanoDSF works well for:

  • scFvs (single-chain variable fragments)
  • FAPs (fluorogen-activating proteins)
  • Nanobodies
  • Certain de novo designed proteins
  • Other proteins with sufficient aromatic amino acid content

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Applications

Stability Assessment

Determine baseline thermal stability and compare protein variants to identify the most stable candidates.

Formulation Support

Evaluate how different buffer conditions affect protein stability to optimize storage and experimental conditions.

Thermostability measurements provide valuable insights into protein behavior and help optimize experimental conditions for downstream applications.