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Related Concept Videos

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
Carbon-13 (¹³C) NMR: Overview01:10

Carbon-13 (¹³C) NMR: Overview

Carbon-13 is a naturally occurring NMR-active isotope of carbon with a low natural abundance of 1.1%. In contrast, carbon-12 is the most abundant isotope of carbon with zero nuclear spin. Therefore, it is NMR inactive. The gyromagnetic ratio of carbon-13 is smaller than that of protons. As a result, carbon-13 resonance is about 6000 times weaker than proton resonance. For a given magnetic field strength, the resonance frequency of carbon-13 is about one-fourth of the resonance frequency for...
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 Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
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...
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...

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Related Experiment Video

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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 refinement using 13C alpha chemical shift tensors.

Benjamin J Wylie1, Charles D Schwieters, Eric Oldfield

  • 1Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.

Journal of the American Chemical Society
|January 7, 2009
PubMed
Summary
This summary is machine-generated.

We developed a new chemical shift tensor (CST) force field for protein structure determination. Incorporating CST restraints into Xplor-NIH improved the accuracy and precision of GB1 protein structures.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Chemistry

Background:

  • Accurate protein structure determination is crucial for understanding biological function.
  • Existing methods for protein structure refinement have limitations in precision and accuracy.

Purpose of the Study:

  • To develop and validate a novel chemical shift tensor (CST) force field for protein structure refinement.
  • To assess the impact of CST restraints on the precision and accuracy of protein structure determination using Xplor-NIH.

Main Methods:

  • Obtained (13)C alpha chemical shift tensors for each amino acid in the protein GB1.
  • Developed a CST force field and integrated it into the Xplor-NIH structure determination program.
  • Compared GB1 structures determined with and without CST restraints, alongside other experimental restraints.

Main Results:

  • GB1 structures refined with CST restraints demonstrated improved precision compared to those without.
  • The inclusion of CST restraints led to more accurate protein structures.
  • Combined with other restraints, CSTs reduced the root-mean squared error to existing X-ray structures to approximately 1.0 Å.

Conclusions:

  • Chemical shift tensors are valuable for protein structure refinement, enhancing both accuracy and precision.
  • This approach facilitates accurate de novo protein structure determination.
  • The developed CST force field and methodology have broad implications for structural biology research.