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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...
¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

¹H NMR of Labile Protons: Deuterium (²H) Substitution

This lesson illustrates the role of deuterium substitution in simplifying the NMR spectrum of compounds comprising labile protons. One method employed is the use of deuterium. Amongst the three isotopes of hydrogen, deuterium (2H) has a nucleus composed of one proton and one neutron. When the D2O solvent is added to a pure dry ethanol solution, its labile proton is substituted with deuterium.
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
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: Jun 6, 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

Homonuclear mixing sequences for perdeuterated proteins.

Kuo-Ying Huang1, Ansgar B Siemer, Ann E McDermott

  • 1Department of Chemistry MC3113, Columbia University, 3000 Broadway, New York, NY 10027, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|November 25, 2010
PubMed
Summary

We compared (13)C homonuclear mixing sequences for solid-state NMR. RFDR showed the best overall efficiency, while DREAM performed exceptionally well in the aliphatic region without proton decoupling.

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Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
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Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

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Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
10:10

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Biomolecular structure determination.
  • Protein dynamics analysis.

Background:

  • Solid-state NMR is crucial for studying insoluble or non-crystalline biomolecules.
  • (13)C homonuclear correlation experiments are vital for resonance assignment and structural analysis.
  • Optimizing these experiments under low-magic angle spinning (MAS) frequencies and without proton decoupling is essential for challenging samples.

Purpose of the Study:

  • To evaluate and compare the performance of various (13)C homonuclear mixing sequences.
  • To identify the most efficient sequence for solid-state NMR of perdeuterated microcrystalline ubiquitin under specific experimental conditions.
  • To assess the utility of DREAM and RFDR sequences in aliphatic spectral regions.

Main Methods:

  • Application of thirteen (13)C homonuclear mixing sequences.
  • Experiments conducted on perdeuterated microcrystalline ubiquitin.
  • Measurements performed without (1)H decoupling at low MAS frequencies.

Main Results:

  • The Radio Frequency Driven Recoupling (RFDR) sequence exhibited the highest overall (13)C spin transfer efficiency.
  • The Dipolar Recoupling Enhanced by Adiabatic Modulation (DREAM) sequence demonstrated superior performance in the aliphatic spectral region.
  • DREAM was found to be approximately twice as efficient as other tested sequences in the aliphatic region.

Conclusions:

  • RFDR is a highly efficient sequence for general (13)C homonuclear correlation in solid-state NMR.
  • DREAM offers significant advantages for spectral editing and analysis in aliphatic regions under low-field, non-decoupled conditions.
  • These findings provide valuable guidance for optimizing solid-state NMR experiments on challenging biomolecular systems.