The protein topography of the E. coli 30S ribosomal subunit: A preliminary model E. coli/30S subunit/ribosome/spatial arrangement of proteins

Tung Tien Sun; Ronald L. Heimark; Robert R. Traut

doi:10.1007/BF01731864

The protein topography of the E. coli 30S ribosomal subunit: A preliminary model E. coli/30S subunit/ribosome/spatial arrangement of proteins

Tung Tien Sun, Ronald L. Heimark, Robert R. Traut

Research output: Contribution to journal › Review article › peer-review

1 Scopus citations

Abstract

A three dimensional model is presented which shows the spatial arrangement of 20 of the 21 proteins of the 30S ribosomal subunit of Escherichia coli. The model fulfills several purposes: (a) It summarizes currently available structural and functional data on ribosomal proteins; (b) It suggests an interesting correlation between stoichiometry and function. Functional proteins are both clustered and fractional; (c) It can be evaluated in relation to new data, and it may predict relationships or point out critical experiments by which it can be tested.

Original language	English (US)
Pages (from-to)	33-41
Number of pages	9
Journal	Molecular and Cellular Biochemistry
Volume	6
Issue number	1
DOIs	https://doi.org/10.1007/BF01731864
State	Published - Jan 1975
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Clinical Biochemistry
Cell Biology

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abstract = "A three dimensional model is presented which shows the spatial arrangement of 20 of the 21 proteins of the 30S ribosomal subunit of Escherichia coli. The model fulfills several purposes: (a) It summarizes currently available structural and functional data on ribosomal proteins; (b) It suggests an interesting correlation between stoichiometry and function. Functional proteins are both clustered and fractional; (c) It can be evaluated in relation to new data, and it may predict relationships or point out critical experiments by which it can be tested.",

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year = "1975",

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AU - Traut, Robert R.

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AB - A three dimensional model is presented which shows the spatial arrangement of 20 of the 21 proteins of the 30S ribosomal subunit of Escherichia coli. The model fulfills several purposes: (a) It summarizes currently available structural and functional data on ribosomal proteins; (b) It suggests an interesting correlation between stoichiometry and function. Functional proteins are both clustered and fractional; (c) It can be evaluated in relation to new data, and it may predict relationships or point out critical experiments by which it can be tested.

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The protein topography of the E. coli 30S ribosomal subunit: A preliminary model E. coli/30S subunit/ribosome/spatial arrangement of proteins

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