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Related Concept Videos

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...
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...
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...
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...

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Updated: May 13, 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

Protein structure determination with paramagnetic solid-state NMR spectroscopy.

Ishita Sengupta1, Philippe S Nadaud, Christopher P Jaroniec

  • 1Department of Chemistry and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.

Accounts of Chemical Research
|March 8, 2013
PubMed
Summary
This summary is machine-generated.

This study introduces a novel paramagnetic solid-state Nuclear Magnetic Resonance (NMR) method for determining protein structures. This technique overcomes limitations of traditional methods by using paramagnetic tags to provide long-distance information, enabling de novo protein fold determination.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Conventional methods like X-ray crystallography and solution-state NMR struggle with certain protein structures.
  • Magic-Angle Spinning (MAS) solid-state NMR is promising but limited by the lack of long-distance restraints.
  • Extracting distances beyond ~5 Å using conventional MAS NMR is challenging.

Purpose of the Study:

  • To develop and validate a new approach for atomic-level structural and dynamic analysis of challenging biological systems.
  • To overcome the limitations of conventional MAS NMR in obtaining long-distance structural information.
  • To demonstrate a general method for de novo protein fold determination using paramagnetic solid-state NMR.

Main Methods:

  • Utilized magic-angle spinning (MAS) solid-state NMR spectroscopy.
  • Incorporated covalently attached paramagnetic tags (nitroxide and EDTA-Cu(2+)) into protein variants.
  • Analyzed paramagnetic relaxation enhancements of nuclear spins as a function of electron-nucleus distance.

Main Results:

  • Successfully determined the global protein fold of a model protein (GB1) using paramagnetic solid-state NMR.
  • Required only a few backbone amide (15)N longitudinal paramagnetic relaxation enhancements per residue.
  • Achieved de novo structure determination without relying on conventional internuclear distance restraints.

Conclusions:

  • Paramagnetic solid-state NMR, using relaxation enhancements, effectively provides long-distance structural restraints.
  • This methodology circumvents the limitations of conventional MAS NMR for challenging protein structures.
  • The approach is general and applicable to larger proteins and protein complexes.