Assignment of the proton NMR spectrum and secondary structure elucidation of the single-stranded DNA binding protein encoded by the filamentous bacteriophage IKe-Reference-Cited by-同舟云学术

Assignment of the proton NMR spectrum and secondary structure elucidation of the single-stranded DNA binding protein encoded by the filamentous bacteriophage IKe

Published:1992-02-01 Issue:4 Volume:31 Page:1254-1262
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Van Duynhoven J. P. M.,Folkers P. J. M.,Prinse C. W. J. M.,Harmsen B. J. M.,Konings R. N. H.,Hilbers C. W.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00119a039

Reference30 articles.

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

2. 1H NMR Studies of the Binding of Bacteriophage-M13-Encoded Gene-5 Protein to Oligo(deoxyadeny1ic acid)s of Varying Length

3. Water suppression in two-dimensional spin-locked NMR experiments using a novel phase-cycling procedure

4. A Preliminary Structure for the DNA Binding Protein From Bacteriophage IKe

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2. Circular Dichroism and Electron Microscopy of a Core Y61F Mutant of the F1 Gene 5 Single-Stranded DNA-Binding Protein and Theoretical Analysis of CD Spectra of Four Tyr → Phe Substitutions;Biochemistry;1998-04-30

3. The Solution Structure of the Synthetic Circular Peptide . NMR Studies of the Folding of a Synthetic Model for the DNA-Binding Loop of the ssDNA-Binding Protein Encoded by Gene V of Phage M13;European Journal of Biochemistry;1996-06-15

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5. Single-stranded DNA binding protein encoded by the filamentous bacteriophage M13: structural and functional characteristics;Molecular Biology Reports;1995