Skip NavigationSkip to Content
Return Return to Search Results

H-1-N-15 correlation spectroscopy of nanocrystalline proteins

  1. Author:
    Morcombe, C. R.
    Paulson, E. K.
    Gaponenko, V.
    Byrd, R. A.
    Zilm, K. W.

  2. Author Address

    Yale Univ, Dept Chem, New Haven, CT 06520 USA. Natl Canc Inst, Struct Biophys Lab, Ft Detrick, MD 21702 USA Zilm, KW, Yale Univ, Dept Chem, POB 208107, New Haven, CT 06520 USA
    1. Year: 2005
    2. Date: MAR
  2. Journal: Journal of Biomolecular Nmr
    1. 31
    2. 3
    3. Pages: 217-230
  4. Type of Article: Article
  1. Abstract:

    The limits of resolution that can be obtained in H-1-N-15 2D NMR spectroscopy of isotopically enriched nanocrystalline proteins are explored. Combinations of frequency switched Lee-Goldburg (FSLG) decoupling, fast magic angle sample spinning (MAS), and isotopic dilution via deuteration are investigated as methods for narrowing the amide H-1 resonances. Heteronuclear decoupling of N-15 from the H-1 resonances is also studied. Using human ubiquitin as a model system, the best resolution is most easily obtained with uniformly H-2 and N-15 enriched protein where the amides have been exchanged in normal water, MAS at ∼ 20 kHz, and WALTZ-16 decoupling of the N-15 nuclei. The combination of these techniques results in average 1H lines of only ∼ 0.26 ppm full width at half maximum. Techniques for optimizing instrument stability and N-15 decoupling are described for achieving the best possible performance in these experiments

    See More

  1. Keywords:

External Sources

  1. View record in Web of Science®
  2. WOS: 000228978300003

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel