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

Solid state NMR: new tools for insight into enzyme function.

Ann McDermott1, Tatyana Polenova

  • 1Columbia University, Department of Chemistry, New York, NY 10027, United States. aem5@columbia.edu

Current Opinion in Structural Biology
|October 30, 2007
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

Structure of the disulfide-rich modules of a striking tandem repeat protein, avian cysteine-rich eggshell membrane protein.

Protein science : a publication of the Protein Society·2025
Same author

Structure of the Disulfide-rich Modules of a Striking Tandem Repeat Protein, Avian Cysteine-Rich Eggshell Membrane Protein.

bioRxiv : the preprint server for biology·2025
Same author

Structural Basis for HIV-1 Maturation Inhibition by PF-46396 Determined by MAS NMR.

Journal of the American Chemical Society·2025
Same author

Pushing Sensitivity and Specificity Limits in Native Structural Biology: <sup>19</sup> F Multinuclear Dynamic Nuclear Polarization with Magic Angle Spinning.

bioRxiv : the preprint server for biology·2025
Same author

Structural Basis for HIV-1 Maturation Inhibition by PF-46396 Determined by MAS NMR.

bioRxiv : the preprint server for biology·2025
Same author

Pushing Sensitivity and Specificity Limits in Native Structural Biology: <sup>19</sup>F Multinuclear Dynamic Nuclear Polarization with Magic Angle Spinning.

Journal of the American Chemical Society·2025

Nuclear Magnetic Resonance (NMR) spectroscopy provides key insights into enzyme mechanisms, including dynamics and electronic states. Solid-state NMR (SSNMR) is a powerful technique for analyzing enzymes, especially membrane-associated or redox-active ones.

Area of Science:

  • Biochemistry
  • Biophysics
  • Spectroscopy

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy has significantly advanced enzymology.
  • It probes enzyme ionization states, conformational strain, interactions, electronic properties, and dynamics.
  • Solid-state NMR (SSNMR) is gaining prominence due to new analytical tools and improved sample isolation.

Purpose of the Study:

  • To review recent applications of NMR, particularly SSNMR, in enzymology.
  • To highlight the utility of SSNMR for studying challenging enzyme systems.
  • To showcase advancements in understanding enzyme mechanisms through spectroscopic methods.

Main Methods:

  • Review of recent literature on NMR and SSNMR studies of enzymes.
  • Focus on applications in Michaelis complex analysis.

Related Experiment Videos

  • Examination of dynamic functioning in membrane-associated enzymes.
  • Analysis of enzymes with redox-active and paramagnetic centers using SSNMR.
  • Main Results:

    • NMR provides critical evidence for enzyme ionization states and conformational dynamics.
    • SSNMR enables detailed analysis of protein structures and functions.
    • Recent studies demonstrate SSNMR's capability in investigating complex enzyme systems like Michaelis complexes and membrane enzymes.
    • SSNMR is effective for enzymes with redox-active and paramagnetic centers.

    Conclusions:

    • NMR spectroscopy is indispensable for understanding enzyme mechanisms.
    • Solid-state NMR (SSNMR) is a rapidly advancing technique crucial for studying enzyme dynamics and function.
    • SSNMR offers unique advantages for analyzing enzymes in their native or near-native states, including membrane-associated and redox-active enzymes.