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    Nat Protoc. 2007;2(9):2212-21.

    The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability.

    Source

    Structural Genomics Consortium, Botnar Research Centre, Oxford University, Oxford, UK. frank.niesen@sgc.ox.ac.uk

    Abstract

    Differential scanning fluorimetry (DSF) is a rapid and inexpensive screening method to identify low-molecular-weight ligands that bind and stabilize purified proteins. The temperature at which a protein unfolds is measured by an increase in the fluorescence of a dye with affinity for hydrophobic parts of the protein, which are exposed as the protein unfolds. A simple fitting procedure allows quick calculation of the transition midpoint; the difference in the temperature of this midpoint in the presence and absence of ligand is related to the binding affinity of the small molecule, which can be a low-molecular-weight compound, a peptide or a nucleic acid. DSF is best performed using a conventional real-time PCR instrument. Ligand solutions from a storage plate are added to a solution of protein and dye, distributed into the wells of the PCR plate and fluorescence intensity measured as the temperature is raised gradually. Results can be obtained in a single day.

    PMID:
    17853878
    [PubMed - indexed for MEDLINE]

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