Polydispersity as a Parameter for Indicating the Thermal Stability of Proteins by Dynamic Light Scattering

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  • SHIBA Kohei
    Department of Applied Chemistry, Faculty of Engineering, Kyushu University Sysmex Corporation
  • NIIDOME Takuro
    Department of Applied Chemistry, Faculty of Engineering, Kyushu University Center for Future Chemistry, Kyushu University PRESTO, Japan Science and Technology Corporation
  • KATOH Etsuko
    Division of Plant Research, National Institute of Agrobiological Sciences
  • XIANG Hongyu
    Division of Plant Research, National Institute of Agrobiological Sciences
  • HAN Lu
    Division of Plant Research, National Institute of Agrobiological Sciences
  • MORI Takeshi
    Department of Applied Chemistry, Faculty of Engineering, Kyushu University Center for Future Chemistry, Kyushu University
  • KATAYAMA Yoshiki
    Department of Applied Chemistry, Faculty of Engineering, Kyushu University Center for Future Chemistry, Kyushu University

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Description

A physical parameter for predicting the thermal stability of proteins was provided by a new approach using dynamic light scattering (DLS). The relationship between the melting point measured by differential scanning calorimetry (DSC) and the polydispersity of the hydrodynamic diameter determined by DLS analysis was examined. Calmodulin (CaM) and concanavalin A (ConA) were used as model proteins. The melting point measured by DSC, an indicator for thermal stability, increased and the polydispersity decreased on binding of the proteins to specific ligands, suggesting that the polydispersity could be used an indicator to predict thermal stability. In addition, the increase of thermal stability that resulted from forming a complex could be quantified by polydispersity analysis even when the melting point changed only slightly.

Journal

  • Analytical Sciences

    Analytical Sciences 26 (6), 659-663, 2010

    The Japan Society for Analytical Chemistry

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