Polydispersity as a parameter for indicating the thermal stability of proteins by dynamic light scattering.
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.
Shiba
Kohei
K
Department of Applied Chemistry, Faculty of Engineering, Kyushu University, 744 Motooka, Nishi, Fukuoka 819-0395, Japan. shiba.kouhei@sysmex.co.jp
Niidome
Takuro
T
Katoh
Etsuko
E
Xiang
Hongyu
H
Han
Lu
L
Mori
Takeshi
T
Katayama
Yoshiki
Y
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000737:chemistry / Q000378:metabolism; D002417:Cattle; D003208:Concanavalin A / Q000737:chemistry; D008027:Light; D008297:Male; D008958:Models, Molecular; D011487:Protein Conformation; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry*; D012542:Scattering, Radiation; D013696:Temperature; D044366:Transition Temperature
D002147:Calmodulin; D011506:Proteins; D003208:Concanavalin A; D002118:Calcium