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Protein Organization01:13

Protein Organization

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Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
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.
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Protein Folding01:25

Protein Folding

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Related Experiment Video

Updated: May 22, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Efficient sequential assignments in proteins with reduced dimensionality 3D HN(CA)NH.

Kousik Chandra1, Garima Jaipuria, Divya Shet

  • 1NMR Research Centre, Indian Institute of Science, Bangalore, 560012, India.

Journal of Biomolecular NMR
|January 10, 2012
PubMed
Summary

We developed a new 3D HN(CA)NH experiment for fast and efficient protein resonance assignment. This method uniquely maps amino acid sequences, proving effective for complex proteins and intrinsically disordered polypeptides.

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Related Experiment Videos

Last Updated: May 22, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

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Published on: July 14, 2015

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09:51

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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

Area of Science:

  • Structural Biology
  • Biophysics
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Sequential assignment of protein resonances is crucial for structural and functional studies.
  • Existing methods can be time-consuming and challenging for certain protein types, such as intrinsically disordered proteins.

Purpose of the Study:

  • To introduce and validate a novel reduced dimensionality (RD) 3D HN(CA)NH experiment.
  • To develop an efficient strategy for sequence-specific resonance assignment using this new technique.

Main Methods:

  • Implementation of the RD 3D HN(CA)NH experiment for rapid acquisition of four-dimensional chemical shift correlations.
  • Integration of HN(CA)NH correlations with amino acid type information from 3D CBCA(CO)NH, categorized by C(beta) chemical shifts.
  • Application of the assignment strategy to diverse systems including maltose binding protein, an intrinsically disordered protein domain, and ubiquitin.

Main Results:

  • The RD 3D HN(CA)NH experiment provides high-resolution data rapidly.
  • A strategy combining HN(CA)NH and CBCA(CO)NH data allows unique sequence assignment with as few as five residues.
  • Successful assignment demonstrated on proteins of varying sizes and structures, including intrinsically disordered proteins.

Conclusions:

  • The RD 3D HN(CA)NH experiment is a powerful tool for high-throughput protein resonance assignment.
  • This method significantly enhances the ability to study unfolded or intrinsically disordered polypeptides.
  • The presented assignment strategy offers a robust approach for sequence-specific resonance mapping.