Polydispersity as a parameter for indicating the thermal stability of proteins by dynamic light scattering

Kohei Shiba; Takuro Niidome; Etsuko Katoh; Hongyu Xiang; Lu Han; Takeshi Mori; Yoshiki Katayama

doi:10.2116/analsci.26.659

Polydispersity as a parameter for indicating the thermal stability of proteins by dynamic light scattering

Kohei Shiba, Takuro Niidome, Etsuko Katoh, Hongyu Xiang, Lu Han, Takeshi Mori, Yoshiki Katayama

Research output: Contribution to journal › Article › peer-review

27 Citations (Scopus)

Abstract

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. 2010

Original language	English
Pages (from-to)	659-663
Number of pages	5
Journal	analytical sciences
Volume	26
Issue number	6
DOIs	https://doi.org/10.2116/analsci.26.659
Publication status	Published - Jun 2010

All Science Journal Classification (ASJC) codes

Analytical Chemistry

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abstract = "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. 2010",

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AU - Shiba, Kohei

AU - Niidome, Takuro

AU - Katoh, Etsuko

AU - Xiang, Hongyu

AU - Han, Lu

AU - Mori, Takeshi

AU - Katayama, Yoshiki

PY - 2010/6

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Polydispersity as a parameter for indicating the thermal stability of proteins by dynamic light scattering

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