Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Nuclear Magnetic Dipole Interactions in Field-Oriented Proteins: Information for Structure Determination in Solution

J. R. Tolman, J. M. Flanagan, M. A. Kennedy and J. H. Prestegard
Proceedings of the National Academy of Sciences of the United States of America
Vol. 92, No. 20 (Sep. 26, 1995), pp. 9279-9283
Stable URL: http://www.jstor.org/stable/2368454
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Nuclear Magnetic Dipole Interactions in Field-Oriented Proteins: Information for Structure Determination in Solution
Preview not available

Abstract

The measurement of dipolar contributions to the splitting of 15N resonances of 1H-15N amide pairs in multidimensional high-field NMR spectra of field-oriented cyanometmyoglobin is reported. The splittings appear as small field-dependent perturbations of normal scalar couplings. Assignment of more than 90 resonances to specific sequential sites in the protein allows correlation of the dipolar contributions with predictions based on the known susceptibility and known structure of the protein. Implications as an additional source of information for protein structure determination in solution are discussed.

Page Thumbnails

  • Thumbnail: Page 
9279
    9279
  • Thumbnail: Page 
9280
    9280
  • Thumbnail: Page 
9281
    9281
  • Thumbnail: Page 
9282
    9282
  • Thumbnail: Page 
9283
    9283