Linking Structure and Function – Use of PDB data as baseline for in-solution characterization

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Poster

Linking Structure and Function – Use of PDB data as baseline for in-solution characterization

Authors

E Stender¹; H Jensen¹;
¹ Fida Biosystems ApS, Denmark

Discussion

Authors

E Stender¹; H Jensen¹;
¹ Fida Biosystems ApS, Denmark

Discussion

In biophysics, the detection of molecular size changes is a strong, quantitative source of information about the structure of a protein and its complexes. However, correlating a protein’s structure to size measures, like Hydrodynamic radius (Rh), requires consideration of structural features of the protein and its assemblies based on either experimental structures or predicted ones by e.g., AlphaFold.

To establish a strong and reliable size baseline, we have developed the Fidabio PDB (Protein Data Bank) Correlator. In the presented work, we use the Fidabio PDB Correlator to predict the in-solution size, Rh, of bovine β-lactoglobulin, human serum albumin, bovine serum albumin and chicken lysozyme. Subsequently, using Fida 1 equipped with a UV fluorescence detector, the Rh of label-free proteins is experimentally determined and compared with the predicted Rh values.