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Structural variability of tRNA: small-angle x-ray scattering of the yeast tRNAphe-Escherichia coli tRNAGlu2 complex.
Proc Natl Acad Sci U S A. 1982 Oct;79(19):5891-5. doi: 10.1073/pnas.79.19.5891.
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Anticodon-anticodon interactions in solution. Studies of the self-association of yeast or Escherichia coli tRNAAsp and of their interactions with Escherichia coli tRNAVal.
J Mol Biol. 1985 Jul 5;184(1):107-118. doi: 10.1016/0022-2836(85)90047-6.
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Anticodon-anticodon interaction induces conformational changes in tRNA: yeast tRNAAsp, a model for tRNA-mRNA recognition.
Proc Natl Acad Sci U S A. 1986 Feb;83(4):932-6. doi: 10.1073/pnas.83.4.932.
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Phenylalanyl-tRNA synthetase from baker's yeast: structural organization of the enzyme and its complex with tRNAPhe as determined by X-ray small-angle scattering.
Z Naturforsch C Biosci. 1979 Jan-Feb;34(1-2):20-6. doi: 10.1515/znc-1979-1-208.
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Imino proton NMR assignments and ion-binding studies on Escherichia coli tRNA3Gly.
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Enzymatic 2'-O-methylation of the wobble nucleoside of eukaryotic tRNAPhe: specificity depends on structural elements outside the anticodon loop.
EMBO J. 1986 May;5(5):1105-9. doi: 10.1002/j.1460-2075.1986.tb04329.x.
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The crystal structure of unmodified tRNAPhe from Escherichia coli.
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Enzymatic conversion of guanosine 3' adjacent to the anticodon of yeast tRNAPhe to N1-methylguanosine and the wye nucleoside: dependence on the anticodon sequence.
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Effect of transfer ribonucleic acid dimer formation on polyphenylalanine biosynthesis.
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Dynamics of transfer RNAs analyzed by normal mode calculation.
Nucleic Acids Res. 1994 Feb 11;22(3):514-21. doi: 10.1093/nar/22.3.514.
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Origin of chirality: a structural theory.
Orig Life. 1984;14(1-4):397-404. doi: 10.1007/BF00933683.
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Conformational dynamics of the anticodon loop in yeast tRNAPhe as sensed by the fluorescence of wybutine.
Eur Biophys J. 1986;13(6):331-42. doi: 10.1007/BF00265669.
5
Anticodon-anticodon interaction induces conformational changes in tRNA: yeast tRNAAsp, a model for tRNA-mRNA recognition.
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6
GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site.
Proc Natl Acad Sci U S A. 1986 Jul;83(13):4617-21. doi: 10.1073/pnas.83.13.4617.
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X-RAY SMALL ANGLE SCATTERING WITH SUBSTANCES OF BIOLOGICAL INTEREST IN DILUTED SOLUTIONS.
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Conformational states of yeast tRNA Phe in the complex with cognate and non cognate synthetases.
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Intramolecular flexibility in phenylalanine transfer RNA.
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Laser light-scattering analysis of the dimerization of transfer ribonucleic acids with complementary anticodons.
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Crystal structure of yeast tRNAAsp.
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Fluorimetric study of the complex between yeast phenylalanyl-tRNA synthetase and tRNA-Phe. 1. Changes in the conformation of the enzyme and tRNA; modification of the Wybutine neighbourhood.
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Nuclear magnetic resonance studies of codon-anticodon interaction in tRNAPhe. I. Effect of binding complementary tetra and pentanucleotides to the anticodon.
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On the conformation of phenylalanine specific transfer RNA. Studies on size and shape of the molecule by x-ray small angle scattering.
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Molecular mechanics of translation: a reciprocating ratchet mechanism.
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