Conformational Changes of Yeast tRNAPhe as Monitored by 31P NMR
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1981.tb06249.x/fullpdf
Reference26 articles.
1. 31P magnetic resonance of tRNA.
2. Studies of yeast phenylalanine-accepting transfer ribonucleic acid backbone structure in solution by phosphorus-31 nuclear magnetic resonance spectroscopy
3. A novel conformational change of the anticodon region of tRNAPhe(yeast)
4. Resolution of five conformational transitions in phenylalaninespecific tRNA from yeast
5. A nuclear magnetic resonance study of secondary and tertiary structure in yeast tRNAPhe
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1. Probing the conformation of human tRNA3Lysin solution by NMR;FEBS Letters;2007-10-24
2. On the conformation of the anticodon loops of initiator and elongator methionine tRNAs;Journal of Molecular Biology;1997-04
3. Imino proton NMR assignments and ion-binding studies on Escherichia coli tRNA3Gly;European Journal of Biochemistry;1986-02
4. Conformation, dynamics, and structural transitions of the TATA box region of the self-complementary d[C-G)n-T-A-T-A-(C-G)n] duplexes in solution;Biochemistry;1985-02
5. Contributions of the PO ester and CO torsion angles of the phosphate group to31P-nuclear magnetic shielding constant in nucleic acids: Theoretical and experimental study of model compounds;Biopolymers;1984-02
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