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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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...
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...

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Related Experiment Video

Updated: Jul 15, 2026

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Microgram-scale protein structure determination by NMR.

James M Aramini1, Paolo Rossi, Clemens Anklin

  • 1Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, and Northeast Structural Genomics Consortium (NESG), Rutgers University, Piscataway, New Jersey 08854, USA.

Nature Methods
|May 15, 2007
PubMed
Summary

Researchers determined the 3D structure of a protein using microgram quantities and advanced nuclear magnetic resonance (NMR) technology. This breakthrough enables structural studies for proteins available in limited amounts.

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

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Area of Science:

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

Background:

  • Determining protein structures is crucial for understanding biological functions.
  • Limited protein availability often hinders structural studies.
  • Microgram quantities of protein present a significant challenge for traditional methods.

Purpose of the Study:

  • To demonstrate the feasibility of obtaining a complete 3D protein structure using microgram quantities.
  • To showcase the utility of microcoil-probe NMR technology for scarce protein samples.
  • To determine the structure of the Methanosarcina mazei TRAM protein.

Main Methods:

  • Utilized conventional triple-resonance nuclear magnetic resonance (NMR) experiments.
  • Employed a 1 mm triple-resonance microcoil NMR probe.
  • Analyzed a 68-residue Methanosarcina mazei TRAM protein sample (72 µg).

Main Results:

  • Achieved near-complete resonance assignments for the TRAM protein.
  • Successfully determined the three-dimensional (3D) structure of the TRAM protein.
  • Established a new precedent for complete solution NMR structures from microgram protein quantities.

Conclusions:

  • Microcoil-probe NMR technology is highly effective for protein structure determination with limited sample amounts.
  • This approach significantly expands the scope of proteins amenable to structural analysis.
  • Enables structural insights into proteins previously inaccessible due to scarcity.