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30S核糖体亚基的计算机模型。

A computer model for the 30S ribosome subunit.

作者信息

Kuntz I D, Crippen G M

出版信息

Biophys J. 1980 Nov;32(2):677-95. doi: 10.1016/S0006-3495(80)85009-0.

Abstract

We describe a computer-generated model for the locations of the 21 proteins of the 30S subunit of the E. coli ribosome. The model uses a new method of incorporating experimental measurements based on a mathematical technique called distance geometry. In this paper, we use data from two sources: immunoelectron microscopy and neutron-scattering studies. The data are generally self-consistent and lead to a set of relatively well-defined structures in which individual protein coordinates differ by approximately 20 A from one structure to another. Two important features of this calculation are the use of extended proteins rather than just the centers of mass, and the ability to confine the protein locations within an arbitrary boundary surface so that only solutions with an approximate 30S "shape" are permitted.

摘要

我们描述了一种计算机生成的大肠杆菌核糖体30S亚基21种蛋白质位置的模型。该模型采用了一种基于称为距离几何学的数学技术来纳入实验测量的新方法。在本文中,我们使用了两个来源的数据:免疫电子显微镜和中子散射研究。这些数据总体上是自洽的,并导致了一组相对明确的结构,其中各个蛋白质的坐标在不同结构之间相差约20埃。该计算的两个重要特征是使用延伸的蛋白质而不仅仅是质心,以及能够将蛋白质位置限制在任意边界表面内,从而只允许具有近似30S“形状”的解决方案。

相似文献

1
A computer model for the 30S ribosome subunit.30S核糖体亚基的计算机模型。
Biophys J. 1980 Nov;32(2):677-95. doi: 10.1016/S0006-3495(80)85009-0.
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1
Spatial configuration of ribosomal proteins: a computer-generated model of the 30S subunit.
Biochem Biophys Res Commun. 1974 Aug 5;59(3):1069-78. doi: 10.1016/s0006-291x(74)80088-4.
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On the computation of the tertiary structure of globular proteins.
J Theor Biol. 1978 Jun 6;72(3):443-57. doi: 10.1016/0022-5193(78)90311-9.
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Distance constraints on macromolecular conformation.大分子构象的距离限制
Int J Pept Protein Res. 1979 Mar;13(3):320-6. doi: 10.1111/j.1399-3011.1979.tb01886.x.
7
Ribosome structure.核糖体结构。
Annu Rev Biochem. 1978;47:217-49. doi: 10.1146/annurev.bi.47.070178.001245.
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Triangulation of proteins in the 30 S ribosomal subunit of Exherichia coli.
J Mol Biol. 1977 May 15;112(2):199-227. doi: 10.1016/s0022-2836(77)80139-3.

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