Rapid Quantification of Protein-Ligand Binding via ¹⁹F NMR Lineshape Analysis.

ABSTRACT: Fluorine incorporation is ideally suited to many NMR techniques, and incorporation of fluorine into proteins and fragment libraries for drug discovery has become increasingly common. Here, we use one-dimensional ¹⁹F NMR lineshape analysis to quantify the kinetics and equilibrium thermodynamics for the binding of a fluorine-labeled Src homology 3 (SH3) protein domain to four proline-rich peptides. SH3 domains are one of the largest and most well-characterized families of protein recognition domains and have a multitude of functions in eukaryotic cell signaling. First, we showe that fluorine incorporation into SH3 causes only minor structural changes to both the free and bound states using amide proton temperature coefficients. We then compare the results from lineshape analysis o

SUBMITTER: Stadmiller SS 

PROVIDER: S-EPMC7231920 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature