Carbon-13 NMR of methylated lysines of fd gene 5 protein: evidence for a conformational change involving lysine 24 upon binding of a negatively charged lanthanide chelate-Reference-Cited by-同舟云学术

Carbon-13 NMR of methylated lysines of fd gene 5 protein: evidence for a conformational change involving lysine 24 upon binding of a negatively charged lanthanide chelate

Published:1989-09-19 Issue:19 Volume:28 Page:7896-7904
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dick Lawrence R.,Geraldes Carlos F. G. C.,Sherry A. Dean,Gray Carla W.,Gray Donald M.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00445a052

Reference27 articles.

1. Isolation and characterization of gene 5 protein of filamentous bacterial viruses

2. 500 MHz 1 H NMR study of the role of lysines and arginines in the binding of gene-5 protein to oligoadenylic acids

3. Fluorescence studies of the complex formation between the gene 5 protein of bacteriophage M13 and polynucleotides

4. A 500MHz proton nuclear magnetic resonance study of the structure and structural alterations of gene-5 protein-oligodeoxyadenylic acid complexes

5. Chemical modifications of functional residues of fd gene 5 DNA-binding protein

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