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Related Concept Videos

Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Folding01:22

Protein Folding

Overview
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: Jun 26, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Proton assisted recoupling and protein structure determination.

Gaël De Paëpe1, Józef R Lewandowski, Antoine Loquet

  • 1Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.

The Journal of Chemical Physics
|January 7, 2009
PubMed
Summary
This summary is machine-generated.

We developed Proton Assisted Recoupling (PAR), a new NMR technique for enhanced polarization transfer between carbon-13 or nitrogen-15 spins. This method improves protein structure determination by revealing longer-range molecular distances.

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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

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Last Updated: Jun 26, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Biophysical Chemistry
  • Structural Biology

Background:

  • Magic Angle Spinning (MAS) NMR is crucial for studying biomolecular structures.
  • High spinning frequencies in modern MAS NMR experiments present challenges for polarization transfer.
  • Existing recoupling mechanisms can be limited in efficiency and scope.

Purpose of the Study:

  • To introduce and characterize a novel homonuclear recoupling technique, Proton Assisted Recoupling (PAR).
  • To enable efficient polarization transfer between (13)C-(13)C or (15)N-(15)N spins in high-field MAS NMR.
  • To demonstrate the utility of PAR for protein structure determination.

Main Methods:

  • Development of a second-order polarization transfer mechanism utilizing proton-heteronuclear couplings.
  • Application of average Hamiltonian theory to derive the effective Hamiltonian for PAR.
  • Analytical and numerical simulations to optimize PAR parameters and understand its behavior.
  • Experimental validation using uniformly (13)C, (15)N labeled microcrystalline Crh protein.

Main Results:

  • PAR effectively mediates zero quantum (13)C-(13)C and (15)N-(15)N recoupling via trilinear spin terms.
  • Optimization maps and matching conditions for PAR were elucidated.
  • PAR demonstrates reduced dipolar truncation, enabling observation of longer internuclear distances (6-7 Å).
  • Successful application of PAR in determining the structure of the Crh protein.

Conclusions:

  • Proton Assisted Recoupling (PAR) is an effective technique for homonuclear spin recoupling in high-field MAS NMR.
  • PAR enhances polarization transfer, facilitating the observation of long-range structural information in proteins.
  • PAR is a valuable tool for advancing protein structure determination using solid-state NMR.