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 Concept Videos

Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Tunable, High-Relaxivity Gd(III)-Conjugated Lipoic Acid Hydrogels for Magnetic Resonance Imaging.

ACS applied materials & interfaces·2026
Same author

An Enzyme-Responsive Gd(III) MRI Probe for Visualizing β-Hexosaminidase A Activity.

ACS sensors·2026
Same author

Recent Trends in Metabolomics by NMR Spectroscopy.

Angewandte Chemie (International ed. in English)·2026
Same author

Machine learning supported olive oil compound profiling for assessing geographic and cultivar authenticity.

Food research international (Ottawa, Ont.)·2026
Same author

Chemical Control of Aggregation-Induced Enhancement via β-Galactose and Gadolinium Chelates.

Inorganic chemistry·2026
Same author

The fine effects of high magnetic fields on hyperfine shifts.

Chemical science·2026

Related Experiment Video

Updated: May 24, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Solid-state NMR crystallography through paramagnetic restraints.

Claudio Luchinat1, Giacomo Parigi, Enrico Ravera

  • 1Magnetic Resonance Center (CERM), University of Florence, via Sacconi 6, Sesto Fiorentino, Italy. luchinat@cerm.unifi.it

Journal of the American Chemical Society
|March 8, 2012
PubMed
Summary

Solid-state NMR spectroscopy (SS-NMR) using pseudocontact shifts (PCSs) on paramagnetic metalloproteins enables NMR crystallography. This method determines both protein structure and crystal packing with high accuracy.

More Related Videos

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Methods of Ex Situ and In Situ Investigations of Structural Transformations: The Case of Crystallization of Metallic Glasses
08:55

Methods of Ex Situ and In Situ Investigations of Structural Transformations: The Case of Crystallization of Metallic Glasses

Published on: June 7, 2018

Related Experiment Videos

Last Updated: May 24, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Methods of Ex Situ and In Situ Investigations of Structural Transformations: The Case of Crystallization of Metallic Glasses
08:55

Methods of Ex Situ and In Situ Investigations of Structural Transformations: The Case of Crystallization of Metallic Glasses

Published on: June 7, 2018

Area of Science:

  • Biophysics
  • Structural Biology
  • Solid-state NMR Spectroscopy

Background:

  • Paramagnetic metalloproteins are crucial for understanding biological processes.
  • Solid-state NMR spectroscopy (SS-NMR) is a powerful technique for studying protein structure.
  • NMR crystallography combines NMR data with crystallographic principles.

Purpose of the Study:

  • To demonstrate the utility of pseudocontact shifts (PCSs) in solid-state NMR for determining protein structures.
  • To validate the application of SS-NMR-derived restraints for accurate crystal packing analysis.

Main Methods:

  • Measurement of pseudocontact shifts (PCSs) in microcrystalline powders of a paramagnetic metalloprotein using SS-NMR.
  • Integration of PCSs with other SS-NMR experimental restraints.
  • Application of NMR crystallography principles to analyze the obtained data.

Main Results:

  • Successful determination of the protein molecular structure using PCSs from SS-NMR.
  • Accurate elucidation of the crystal packing of the studied metalloprotein.
  • Demonstration that PCSs provide valuable long-range structural information.

Conclusions:

  • PCSs measured by SS-NMR are effective restraints for NMR crystallography.
  • This approach allows for the simultaneous determination of protein structure and crystal packing.
  • NMR crystallography using SS-NMR offers a complementary method to traditional X-ray crystallography.