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刀豆球蛋白酪氨酸残基的光谱研究。

Spectroscopic studies on the tyrosine residues of canavalin.

作者信息

Margalit R, Shaklai N

出版信息

Biochim Biophys Acta. 1978 Aug 21;535(2):272-80. doi: 10.1016/0005-2795(78)90093-4.

Abstract

Canavalin is a tetramer with 6 tyrosines per subunit. In the work presented here, we have classified these tyrosines by their spectrophotometric and fluorometric pH titration and their ability to be quenched I-. Of the 6 residues, 2 were found to be exposed to the solvent. One (pK = 10.2) contributes 28% of the total fluorescence intensity; the second has a pK of 11.50, and a lower quantum yield, contributing only 16% of the total intensity. The remaining 4 residues (pK = 12.5, contributing 54% of fluorescence intensity) are buried; their titration is irreversible, requiring protein denaturation.

摘要

伴刀豆球蛋白是一种四聚体,每个亚基含有6个酪氨酸。在本文所展示的研究中,我们通过分光光度法和荧光pH滴定以及它们被I-淬灭的能力对这些酪氨酸进行了分类。在这6个残基中,有2个被发现暴露于溶剂中。其中一个(pK = 10.2)贡献了总荧光强度的28%;另一个的pK为11.50,量子产率较低,仅贡献总强度的16%。其余4个残基(pK = 12.5,贡献54%的荧光强度)被掩埋;它们的滴定是不可逆的,需要蛋白质变性。

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