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

Isotope-Filtered Affinity NMR

Gonnella1, Lin, Shapiro

  • 1Preclinical Research, Novartis Pharmaceuticals Corporation, 556 Morris Avenue, Summit, New Jersey, 07901

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|May 8, 1998
PubMed
Summary
This summary is machine-generated.

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

Phase separation of binary mixtures in shear flow: A numerical study

Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics·2001
Same author

Structure and rheology of binary mixtures in shear flow

Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics·2000
Same author

Blue light and abscisic acid independently induce heterophyllous switch in marsilea quadrifolia

Plant physiology·1999
Same author

Thalprzewalskiinone, a new oxobenzylisoquinoline alkaloid from thalictrum przewalskii

Journal of natural products·1999
Same author

Estrogen receptors and glucocorticoid receptors in human well-differentiated thyroid cancer.

International journal of molecular medicine·1998
Same author

Absorption Intensity of Stretching Overtone States of Silane and Germane.

Journal of molecular spectroscopy·1998
Same journal

Localization-driven exchange contrast in diffusion exchange spectroscopy.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

4.5 Tesla superconducting miniature magnet in liquid nitrogen.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Folding and unfolding dynamics of a DNA aptamer studied by heteronuclear <sup>1</sup>H-<sup>13</sup>C correlation zz-exchange spectroscopy.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Multi-spin control from one-spin pulses.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Altering MRI rotating frame relaxations by changing the truncation level of Hyperbolic Secant pulse.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same journal

Effects of proton exchange on the lifetimes of long-lived states in aliphatic chains.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
See all related articles

A new NMR technique directly observes protein-binding ligands in complex mixtures. This method aids pharmaceutical lead compound discovery by eliminating signals from proteins and non-binding molecules.

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Structural Biology

Background:

  • Identifying specific binding interactions is crucial for drug discovery.
  • Distinguishing bound ligands from free ligands in complex biological mixtures is challenging.
  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for molecular analysis.

Purpose of the Study:

  • To develop a novel NMR pulse sequence for direct observation of protein-binding ligands.
  • To facilitate the identification of lead pharmaceutical compounds.
  • To overcome limitations of existing methods in analyzing complex mixtures.

Main Methods:

  • Development of a double-editing NMR pulse sequence.
  • Utilizing 13C isotope editing to suppress protein signals.

Related Experiment Videos

  • Employing Pulsed Field Gradient (PFG) diffusion-editing to remove non-binding ligand signals.
  • Demonstration on 13C/15N-labeled stromelysin catalytic domain (SCD).

    • Main Results:

    • Successful direct observation of protein-binding ligands from a mixture.
    • Simultaneous elimination of proton NMR signals from both the protein and non-binding ligands.
    • Validation of the technique using a well-characterized protein system.

    Conclusions:

    • The developed double-editing NMR technique enables direct detection of binding ligands.
    • This method significantly aids in the discovery of potential pharmaceutical compounds.
    • The technique offers a robust approach for analyzing ligand-protein interactions in complex systems.