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Home / Equine Research Bank / Biochem Biophys Res Commun / 1H NMR resonance assignments in a paramagnetic heme protein ...
Biochemical and biophysical research communications1991; 175(2); 515-519; doi: 10.1016/0006-291x(91)91594-3

1H NMR resonance assignments in a paramagnetic heme protein by two-dimensional spectroscopy: heme resonances in equine met-azido myoglobin.

Abstract: Specific heme protons for the majority of resonances in the downfield resolved region of equine met-azido myoglobin have been assigned using solely the two-dimensional 1H NMR experiments NOESY and COSY. Metazido myoglobin provides a useful test case for the applicability of these techniques to paramagnetic proteins for the following reasons. First met-azido myoglobin is a mixed spin-state protein, with significantly shorter relaxation times and broadened lines relative to pure low-spin systems (eg., met-cyano myoglobin). Second, met-azido hemoglobin and met-azido myoglobin are important as models for the physiological forms of hemoglobin. Third, a few sperm whale met-azido myoglobin resonances have been previously assigned, which permits a comparison of assignments for these similar proteins, and a check of the method presented here.
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Publication Date: 1991-03-15 PubMed ID: 2018499DOI: 10.1016/0006-291x(91)91594-3Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research focuses on identifying specific heme protons in equine met-azido myoglobin using two-dimensional 1H NMR experiments. This kind of study offers valuable insights into understanding mixed spin-state proteins and developing models for physiological forms of hemoglobin.

Understanding the Research

  • The research was conducted to assign specific heme protons to their corresponding resonances in the ‘downfield resolved region’ of the protein ‘equine met-azido myoglobin’. This was done using two-dimensional 1H NMR experiments called NOESY and COSY.
  • The application of this identification or assignment process is particularly useful for examining paramagnetic proteins, which are proteins that are affected by magnetic fields. The two-dimensional 1H NMR spectroscopy technique can be used to study these proteins in greater detail.

    • Why Met-Azido Myoglobin is Used

  • Equine met-azido myoglobin was chosen as the protein for the study as it provides several advantages for testing the applicability of NOESY and COSY techniques.
  • The first reason is that met-azido myoglobin shows mixed spin-state properties. This means that it has both shorter relaxation times and broader lines compared to pure low-spin systems, providing a more challenging test for the techniques used.
  • The second reason is that met-azido hemoglobin and met-azido myoglobin are useful as models for physiological forms of hemoglobin. Hemoglobin is the protein that carries oxygen in the blood, and understanding its structure and properties is important for many areas of medical and biological research.

    • Usefulness of Previous Research Data

  • The third factor is that there have been previous assignments of resonances in the protein sperm whale met-azido myoglobin. This allows for comparison between the results generated by this study and previous research data, enabling the researchers to verify the accuracy and reliability of their method.
  • The researchers in this study can check their method of resonance assignment against previously established data, ensuring their work is in line with existing scientific understanding.

    • Cite This Article

    APA
    Peyton DH. (1991). 1H NMR resonance assignments in a paramagnetic heme protein by two-dimensional spectroscopy: heme resonances in equine met-azido myoglobin. Biochem Biophys Res Commun, 175(2), 515-519. https://doi.org/10.1016/0006-291x(91)91594-3

    Publication

    Biochemical and biophysical research communications
    ISSN: 0006-291X
    NlmUniqueID: 0372516
    Country: United States
    Language: English
    Volume: 175
    Issue: 2
    Pages: 515-519

    Researcher Affiliations

    Peyton, D H
    • Chemistry Department, Portland State University, Oregon 97207-0751.

    MeSH Terms

    • Animals
    • Azides
    • Hemeproteins / chemistry
    • Horses
    • Magnetic Resonance Spectroscopy / methods
    • Metmyoglobin / chemistry

    Citations

    This article has been cited 1 times.
    1. Ma LH, Liu Y, Zhang X, Yoshida T, La Mar GN. 1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.. J Inorg Biochem 2009 Jan;103(1):10-9.
      doi: 10.1016/j.jinorgbio.2008.08.012pubmed: 18976815google scholar: lookup
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