| Literature DB >> 20543496 |
Kohei Shiba1, Takuro Niidome, Etsuko Katoh, Hongyu Xiang, Lu Han, Takeshi Mori, Yoshiki Katayama.
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.Entities:
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Year: 2010 PMID: 20543496 DOI: 10.2116/analsci.26.659
Source DB: PubMed Journal: Anal Sci ISSN: 0910-6340 Impact factor: 2.081