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肌质网Ca2+-ATP酶二级结构的傅里叶变换红外光谱研究

Fourier transform infrared spectroscopic studies on the secondary structure of the Ca2+-ATPase of sarcoplasmic reticulum.

作者信息

Villalain J, Gomez-Fernandez J C, Jackson M, Chapman D

机构信息

Departamento de Bioquimica, Universidad de Murcia, Spain.

出版信息

Biochim Biophys Acta. 1989 Jan 30;978(2):305-12. doi: 10.1016/0005-2736(89)90129-6.

DOI:10.1016/0005-2736(89)90129-6
PMID:2521561
Abstract

Fourier transform infrared spectroscopy has been applied to the study of the secondary structure of the Ca2+-ATPase of sarcoplasmic reticulum. An attempt is made to quantitatively assess the various secondary structures present. Values of 45% alpha-helix, 32% beta-sheet and 23% turns were obtained. A comparison is made of these results and those obtained using other techniques such as CD and Raman spectroscopy. The various assumptions inherent in the present procedure are discussed. The effect of various ligands, e.g. Ca2+, vanadate, ATP and phosphate, upon the structure were investigated. Upon binding these ligands no marked spectral changes were observed.

摘要

傅里叶变换红外光谱已应用于肌质网Ca2+-ATP酶二级结构的研究。尝试对存在的各种二级结构进行定量评估。得到了45%的α-螺旋、32%的β-折叠和23%的转角值。将这些结果与使用其他技术(如圆二色光谱和拉曼光谱)获得的结果进行了比较。讨论了本方法中固有的各种假设。研究了各种配体(如Ca2+、钒酸盐、ATP和磷酸盐)对结构的影响。结合这些配体后,未观察到明显的光谱变化。

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引用本文的文献

1
A time-resolved Fourier transformed infrared difference spectroscopy study of the sarcoplasmic reticulum Ca(2+)-ATPase: kinetics of the high-affinity calcium binding at low temperature.肌浆网Ca(2+)-ATP酶的时间分辨傅里叶变换红外差光谱研究:低温下高亲和力钙结合的动力学
Biophys J. 1996 Dec;71(6):2970-83. doi: 10.1016/S0006-3495(96)79537-1.