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Related Concept Videos

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...
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...
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...
Inductive Effects on Chemical Shift: Overview01:27

Inductive Effects on Chemical Shift: Overview

The protons in unsubstituted alkanes are strongly shielded with chemical shifts below 1.8 ppm. Methine, methylene, and methyl protons appear at approximately 1.7, 1.2 and 0.7 ppm, while the proton signal from methane appears at 0.23 ppm. An electronegative substituent, such as chlorine, withdraws the electron density from the protons, increasing their chemical shift. Progressive substitution of the hydrogens in methane by chlorine shifts the proton signals increasingly downfield, to 3.05 ppm 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...
¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons01:03

¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons

Protons in identical electronic environments within a molecule are chemically equivalent and have the same chemical shift. The replacement test is a useful tool to identify chemical equivalence and predict NMR spectra. A substituent replaces each of the protons being examined and the resulting molecules are compared. If the same molecule is obtained, the protons are equivalent or homotopic. Replacement of any hydrogens in ethane by chlorine yields chloroethane because all six protons are...

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Related Experiment Video

Updated: May 9, 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

Improving 3D structure prediction from chemical shift data.

Gijs van der Schot1, Zaiyong Zhang, Robert Vernon

  • 1Computational Structural Biology, Bijvoet Center for Biomolecular Research, Faculty of Science-Chemistry, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.

Journal of Biomolecular NMR
|August 6, 2013
PubMed
Summary
This summary is machine-generated.

We improved protein structure prediction using only nuclear magnetic resonance chemical shifts. Enhanced methods yield accurate protein models in 70% of cases, advancing structural biology.

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A Protocol for Computer-Based Protein Structure and Function Prediction
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Last Updated: May 9, 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

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Chemistry

Background:

  • Protein structure determination is crucial for understanding biological function.
  • Nuclear Magnetic Resonance (NMR) spectroscopy provides valuable data for structure calculation.
  • Previous methods like CS-Rosetta showed promise but required further refinement.

Purpose of the Study:

  • To enhance the accuracy and reliability of protein structure calculation using only NMR chemical shift data.
  • To improve the CS-Rosetta method through algorithmic and data processing advancements.
  • To establish robust criteria for assessing the quality of predicted protein structures.

Main Methods:

  • Utilizing an improved fragment picker for selecting structural components.
  • Implementing the iterative sampling algorithm RASREC for enhanced structure assembly.
  • Developing and applying new criteria for evaluating the accuracy of calculated models.

Main Results:

  • Significant improvements in convergence and accuracy of protein structure calculations were achieved.
  • The refined method successfully predicted reliable protein structures in 70% of test cases.
  • All structures passing the reliability filter demonstrated high accuracy, with RMSD < 2 Å.

Conclusions:

  • The enhanced CS-Rosetta method provides a reliable approach for protein structure determination from NMR chemical shifts alone.
  • Improved fragment selection and sampling algorithms are key to advancing NMR-based structure prediction.
  • The developed reliability criteria effectively identify accurate protein models, facilitating structural biology research.