Experimental studies of protein binding affinity by different methods.

POSTER

Abstract

Protein-protein binding is central to most protein functions; convenient assays of binding affinity are thus invaluable for elucidating mechanisms of biological processes. We are carrying out different assays on the binding of the 12 kD FK506-binding protein (FKBP12) with target peptides. The methods include affinity chromatography, isothermal titration calorimetry, and fluorescence spectroscopy. The goal is to identify a convenient protocol for identifying peptides that form part of the binding site on the target protein of FKBP12. FKBP12 is a multiple-function protein. For example, it regulates the ryanodine receptor, a calcium release channel implicated in excitation-contraction coupling. Our approach is expected to have wide applicability in identifying target peptides.

Authors

  • Debangshu Samanta

    Institute of Molecular Biophysics, Department of Physics, Florida State University

  • Daniel Spencer

    Institute of Molecular Biophysics, Florida State University

  • Huan-Xiang Zhou

    Physics Department, Institute of Molecular Biophysics, Institute of Molecular Biophysics and Department of Physics, Florida State University, Tallahassee, FL 32306, Department of Physics and Institute of Molecular Biophysics and School of Computational Science, Florida State University, Tallahassee, FL 32306, Inst. of Mol. Biophys. and Dept. of Phys. Florida State Univ., Institute of Molecular Biophysics, Department of Physics, Florida State University, Institute of Molecular Biophysics \& Department of Physics, Florida State University, Florida State University, Institute of Molecular Biophysics and Department of Physics