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Protein Organization

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....

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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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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Published on: September 17, 2017

Sparse labeling of proteins: structural characterization from long range constraints.

James H Prestegard¹, David A Agard², Kelley W Moremen¹

¹Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, United States.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)

|March 25, 2014

Summary

Sparse isotopic labeling offers a novel approach for protein structural characterization, overcoming resolution challenges in large or non-bacterially expressed biomolecules. This method enhances structural biology insights for complex systems.

Keywords:

Glycoprotein Ligand docking NMR assignments Paramagnetic constraints Protein NMR Residual dipolar coupling Sparse labeling

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Last Updated: May 1, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Published on: September 17, 2017

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Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

Area of Science:

Structural Biology
Biophysics
Biochemistry

Background:

Increasing molecular size in proteins leads to resolution degradation in structural characterization.
Loss of resolution-improving tools like perdeuteration occurs when using non-bacterial expression hosts.
These challenges hinder the structural biology of many important proteins.

Purpose of the Study:

To present an alternative approach for structural characterization of challenging protein systems.
To discuss the potential applications of sparse isotopic labeling and paramagnetic constraints.
To explore future prospects in structural biology for understanding complex biomolecules.

Main Methods:

Utilizing sparse isotopic labeling (single or small subsets of amino acids).
Incorporating long-range paramagnetic constraints.
Employing improved computational modeling for structural analysis.

Main Results:

Demonstrated potential for analyzing very large systems (e.g., Hsp90 homolog) using perdeuteration and methyl-TROSY.
Showcased resolution enhancement via single amino acid labeling for ligand placement in glycosylated proteins (ST6Gal1).
Highlighted the viability of sparse labeling as a powerful alternative to traditional methods.

Conclusions:

Sparse isotopic labeling combined with paramagnetic constraints and computational modeling offers a promising strategy.
This approach effectively addresses resolution limitations in structural biology.
It holds significant potential for advancing the study of complex and challenging biological systems.