Circular dichroism and 500-MHz proton magnetic resonance studies of the interaction of Escherichia coli translational initiation factor 3 protein with the 16S ribosomal RNA 3' cloacin fragment-Reference-Cited by-同舟云学术

Circular dichroism and 500-MHz proton magnetic resonance studies of the interaction of Escherichia coli translational initiation factor 3 protein with the 16S ribosomal RNA 3' cloacin fragment

Published:1986-05-20 Issue:10 Volume:25 Page:2770-2777
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wickstrom Eric,Heus Hans A.,Haasnoot Cornelis A. G.,Van Knippenberg Peter H.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00358a005

Reference54 articles.

1. The 3′-terminus of 16 S ribosomal RNA ofEscherichia coli. Isolation and purification of the terminal 49-nucleotide fragment at a milligram scale

2. High-resolution proton magnetic resonance study of the secondary structure of the 3'-terminal 49-nucleotide fragment of 16S rRNA from Escherichia coli.

3. Formylmethionyl-tRNA binding to 30 S ribosomes programmed with homopolynucleotides and the effect of translational initiation factor 3

4. Circular dichroism study of nine species of transfer ribonucleic acid

5. Comparative optical property studies on polycistronic R17 phage ribonucleic acid and rabbit globin messenger ribonucleic acid

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