Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

An NMR approach to tRNA tertiary structure in solution.

G T Robillard, C E Tarr, F Vosman

    Biophysical Chemistry
    |April 1, 1977
    PubMed
    Summary

    Atomic coordinates for E. Coli tRNA1Val were determined using X-ray crystallography. This study provides a structural model for this essential transfer RNA molecule.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    The SC3 hydrophobin self-assembles into a membrane with distinct mass transfer properties.

    Biophysical journal·2005
    Same author

    Probing the self-assembly and the accompanying structural changes of hydrophobin SC3 on a hydrophobic surface by mass spectrometry.

    Biophysical journal·2004
    Same author

    Structural changes and molecular interactions of hydrophobin SC3 in solution and on a hydrophobic surface.

    Protein science : a publication of the Protein Society·2002
    Same author

    NMR structure of cysteinyl-phosphorylated enzyme IIB of the N,N'-diacetylchitobiose-specific phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.

    Journal of molecular biology·2001
    Same author

    Cysteine cross-linking defines part of the dimer and B/C domain interface of the Escherichia coli mannitol permease.

    The Journal of biological chemistry·2001
    Same author

    Sensitive monitoring of the dynamics of a membrane-bound transport protein by tryptophan phosphorescence spectroscopy.

    Biochemistry·2000

    Area of Science:

    • Structural Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Transfer RNAs (tRNAs) are crucial molecules for protein synthesis, translating genetic code into proteins.
    • The three-dimensional structure of tRNAs is essential for their function.
    • Specific tRNA structures, like E. Coli tRNA1Val, are targets for understanding cellular processes.

    Purpose of the Study:

    • To generate atomic coordinates for Escherichia coli transfer RNA 1, valine (tRNA1Val).
    • To utilize X-ray crystallography data from a related molecule to model the target tRNA.
    • To provide a high-resolution structural model for E. Coli tRNA1Val.

    Main Methods:

    • Atomic coordinates were derived from the known X-ray crystal structure of Yeast tRNAPhe.
    • Base substitutions were computationally performed to convert Yeast tRNAPhe to E. Coli tRNA1Val.
    • Idealization of the resulting atomic model was carried out to refine the structure.

    Main Results:

    • A detailed atomic model representing the three-dimensional structure of E. Coli tRNA1Val was successfully generated.
    • The generated coordinates provide insights into the specific structural features of E. Coli tRNA1Val.
    • The study presents a validated structural representation of this key transfer RNA.

    Conclusions:

    • The atomic coordinates of E. Coli tRNA1Val have been successfully generated through computational modification of a related crystal structure.
    • This structural model serves as a valuable resource for further biochemical and structural studies of E. Coli tRNA1Val.
    • The findings contribute to the broader understanding of tRNA structure-function relationships in prokaryotes.

    Related Experiment Videos