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Milk Proteins pp 133-142 | Cite as

Analysis of Protein Structure in Solution by Two-Dimensional NMR Spectroscopy: 2D-1H NMR Investigation of Ribonuclease T1 and Its Complexes with 2′- and 3′-Guanosine Monophosphates

  • H. Rüterjans
  • E. Hoffmann
  • J. Schmidt
  • J. Simon

Abstract

Two-dimensional (2 D) NMR spectroscopy may be used to study the tertiary structure of proteins and nucleic acids [28]. This NMR approach to determining the structure of biological macromolecules has some advantages over the conventional method using x-ray crystallography:
  1. 1)

    NMR spectroscopy can be applied to proteins that cannot be crystallized;

     
  2. 2)

    The tertiary structure of proteins or nucleic acids can be obtained under varying conditions such as pH, temperature, or inhibitor concentration;

     
  3. 3)

    NMR parameters may provide information on the dynamics of protein conformation, so that exchange processes and molecular flexibility may be studied.

     

Keywords

Cross Peak Proton Resonance Guanosine Monophosphates Cosy Spectrum Coherence Transfer 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Dr. Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1989

Authors and Affiliations

  • H. Rüterjans
    • 1
  • E. Hoffmann
    • 1
  • J. Schmidt
    • 1
  • J. Simon
    • 1
  1. 1.Institute of Biophysical ChemistryJohann Wolfgang Goethe UniversityFrankfurtGermany

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