利用圆二色光谱法和傅里叶变换红外光谱法对鸡骨基质中两种磷蛋白在溶液中的二级结构进行的初步研究。

Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by circular dichroism and fourier transform-infrared spectroscopy.

作者信息

Renugopalakrishnan V, Uchiyama A, Horowitz P M, Rapaka R S, Suzuki M, Lefteriou B, Glimcher M J

出版信息

Calcif Tissue Int. 1986 Sep;39(3):166-70. doi: 10.1007/BF02555113.

Abstract

The secondary structures of two phosphoproteins from chicken bone matrix of Mr approximately 15kDa and approximately 28kDa, rich in Asx, Glx, and Ser, and containing Ser(P) and Thr(P) residues, have been investigated in solution by Circular Dichroism (CD) and Fourier Transform-Infrared Spectroscopy (FT-IR). CD spectroscopy, which yields useful information on the backbone conformation of polypeptides and proteins, suggests a predominantly beta-sheet structure for the two phosphoproteins. The FT-IR spectra of the approximately 15kDa protein, which is sensitive to secondary structure and hence provides complimentary information to CD spectroscopy, are consistent with the results obtained by CD studies.

摘要

对来自鸡骨基质的两种磷蛋白的二级结构进行了研究，这两种磷蛋白分子量约为15kDa和约28kDa，富含天冬氨酸、谷氨酸和丝氨酸，并含有磷酸丝氨酸和磷酸苏氨酸残基，研究方法为溶液中的圆二色性（CD）和傅里叶变换红外光谱（FT-IR）。CD光谱可提供有关多肽和蛋白质主链构象的有用信息，表明这两种磷蛋白主要为β-折叠结构。约15kDa蛋白质的FT-IR光谱对二级结构敏感，因此可为CD光谱提供补充信息，其结果与CD研究所得结果一致。