The conformational stability of ribosomal proteins L7 and L12 fromE. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents-Reference-Cited by-同舟云学术

The conformational stability of ribosomal proteins L7 and L12 fromE. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents

Published:1973-09 Issue:9 Volume:12 Page:2083-2092
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Boublik Miloslav,Brot Nathan,Weissbach Herbert

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference31 articles.

1. Characterization of an acidic protein in 50 s ribosomes ofE. coli

2. Ribosomal proteins. Secondary structure of individual ribosomal proteins of E. coli studied by circular dichroism

3. 50-S Ribosomal Proteins. Purification and Partial Characterization of Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coli

4. 50-S Ribsomal Proteins. Peptide Studies on Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coli

5. Ribosomal proteins

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