:Spectroscopic study of conformation changes of bovine serum albumin in aqueous environment论文

:Spectroscopic study of conformation changes of bovine serum albumin in aqueous environment论文

本文主要研究内容

作者(2019)在《Spectroscopic study of conformation changes of bovine serum albumin in aqueous environment》一文中研究指出:The secondary structural changes of bovine serum albumin(BSA)aqueous solutions with and without calcium cations were investigated by attenuated total reflection-Fourier transform infrared(ATR-FTIR)technology.The spectra of BSA solution and BSA dry powder were mainly reflected the formation of hydrogen bonds between water and BSA.Further investigation indicated that the concentrations of calcium cations in BSA aqueous solution also affected the secondary structural change of the protein.Amide I band was red shifted and amide II band was blue shifted in aqueous enviro nment compared with the d ry BSA powder,and the addition of calcium cations further changed the amide bands position,which led to the change of the secondary structure.The result was coinciding with the Raman spectroscopy.

Abstract

The secondary structural changes of bovine serum albumin(BSA)aqueous solutions with and without calcium cations were investigated by attenuated total reflection-Fourier transform infrared(ATR-FTIR)technology.The spectra of BSA solution and BSA dry powder were mainly reflected the formation of hydrogen bonds between water and BSA.Further investigation indicated that the concentrations of calcium cations in BSA aqueous solution also affected the secondary structural change of the protein.Amide I band was red shifted and amide II band was blue shifted in aqueous enviro nment compared with the d ry BSA powder,and the addition of calcium cations further changed the amide bands position,which led to the change of the secondary structure.The result was coinciding with the Raman spectroscopy.

论文参考文献

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