通过硫的反常散射直接确定的疏水蛋白胰凝乳蛋白酶原的结构。
Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur.
作者信息
Hendrickson Wayne A, Teeter Martha M
机构信息
Laboratory for the Structure of Matter, Naval Research Laboratory 6030, Washington DC 20375, USA.
Department of Chemistry, Boston University, 685 Commonwealth Avenue, Boston, Massachusetts 02215, USA.
出版信息
Nature. 1981 Mar 12;290(5802):107-113. doi: 10.1038/290107a0.
Abstract
The highly ordered crystal structure of crambin has been solved at 1.5 Å resolution directly from the diffraction data of a native crystal at a wavelength remote from the sulphur absorption edge. The molecule has three disulphide bridges among its 46 amino acid residues, of which 46% are in helices and 17% are in a β-sheet. Crambin is shown to be an amphipathic protein, inasmuch as its six charged groups are segregated from hydrophobic surface elements. Phasing methods used here will also apply elsewhere.
摘要
已直接从天然晶体在远离硫吸收边缘的波长下的衍射数据中，以1.5埃的分辨率解析出了胰凝乳蛋白酶原的高度有序晶体结构。该分子在其46个氨基酸残基中有三个二硫键，其中46%处于螺旋结构，17%处于β折叠结构。已证明胰凝乳蛋白酶原是一种两亲性蛋白质，因为其六个带电基团与疏水表面元件分隔开。这里使用的相位测定方法也将适用于其他地方。
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