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

NH-NH vector correlation in peptides by solid-state NMR.

B Reif1, M Hohwy, C P Jaroniec

  • 1Department of Chemistry and MIT/Harvard Center for Magnetic Resonance, Cambridge, Massachusetts, 02139, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|June 30, 2000
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

Time domain DNP at 1.2 T.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2021
Same author

Frequency-Swept Integrated and Stretched Solid Effect Dynamic Nuclear Polarization.

The journal of physical chemistry letters·2018
Same author

High-precision measurement of the electron spin g factor of trapped atomic nitrogen in the endohedral fullerene N@C<sub>60</sub>.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2018
Same author

Overhauser effects in non-conducting solids at 1.2 K.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2017
Same author

Reprint of: Localization of Cl-35 Nuclei in Biological Solids using Rotational-Echo Double-Resonance Experiments.

Solid state nuclear magnetic resonance·2017
Same author

Ramped-amplitude NOVEL.

The Journal of chemical physics·2017

We developed a new solid-state NMR method to measure NH-NH angles in peptides, crucial for determining backbone structure. This technique accurately reveals peptide conformation using magic angle spinning and specific recoupling schemes.

Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy
  • Structural biology
  • Peptide chemistry

Background:

  • Determining peptide backbone structure is essential for understanding their function.
  • Solid-state NMR is a powerful tool for analyzing biomolecular structures.
  • Measuring inter-residue distances and angles provides key structural information.

Purpose of the Study:

  • To present a novel solid-state magic angle-spinning NMR method for measuring the NH(i)-NH(i+1) projection angle in peptides.
  • To relate this projection angle to peptide backbone torsion angles phi(i) and psi(i).
  • To demonstrate the method's applicability to uniformly (15)N-labeled peptides.

Main Methods:

  • Utilizes a novel solid-state magic angle-spinning NMR experiment.

Related Experiment Videos

  • Employs the T-MREV recoupling scheme to restore (15)N-(1)H interactions.
  • Incorporates proton-mediated spin diffusion for (15)N-(15)N correlations.
  • Applies gamma-encoding to enhance the dynamic range of (15)N-(1)H recoupling.

    • Main Results:

    • Successfully measured the NH(i)-NH(i+1) projection angle (θ(i,i+1)) in peptides.
    • Demonstrated the method on the chemotactic tripeptide N-formyl-l-Met-l-Leu-l-Phe.
    • Established a direct relationship between the measured projection angle and peptide backbone torsion angles.
    • Accurately determined the recoupled NH dipolar interaction.

    Conclusions:

    • The novel solid-state NMR method provides an accurate means to measure peptide backbone structural parameters.
    • The quasi-analytical interpretation allows for efficient extraction of structural information.
    • This technique offers a valuable tool for peptide structure determination in the solid state.