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Related Concept Videos

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...

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Related Experiment Video

Updated: May 13, 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

Solution NMR and computational methods for understanding protein allostery.

Gregory Manley1, Ivan Rivalta, J Patrick Loria

  • 1Department of Chemistry, Yale University, New Haven, Connecticut 06520, United States.

The Journal of Physical Chemistry. B
|March 1, 2013
PubMed
Summary

Allosteric regulation in enzymes, crucial for biological control, remains mechanistically unclear. This study uses NMR and computational methods to reveal how imidazole glycerol phosphate synthase allostery functions.

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

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Area of Science:

  • Biochemistry and enzymology
  • Structural biology
  • Biophysics

Background:

  • Allosterism is a fundamental biological regulatory mechanism controlling enzyme activity.
  • Allosteric regulation involves metabolite binding at sites distant from the catalytic site, influencing enzyme function through structural and dynamic changes.
  • The precise mechanisms of allosteric site-to-active site communication are complex and not fully understood for many enzymes.

Purpose of the Study:

  • To elucidate the mechanistic underpinnings of allosteric regulation in imidazole glycerol phosphate synthase.
  • To investigate the interplay between distant allosteric sites and the enzyme's active site.
  • To demonstrate the utility of integrated spectroscopic and computational approaches for studying allosteric enzymes.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy to probe enzyme structure and dynamics.
  • Molecular dynamics (MD) simulations to model protein conformational changes.
  • Network modeling to analyze communication pathways within the enzyme.

Main Results:

  • Detailed characterization of conformational rearrangements in response to allosteric ligand binding.
  • Identification of key residues and pathways mediating allosteric signal transmission.
  • Validation of the integrated NMR and computational approach for dissecting allosteric mechanisms.

Conclusions:

  • The study provides novel mechanistic insights into allostery in imidazole glycerol phosphate synthase.
  • Integrated NMR and computational methods offer a powerful strategy for studying complex allosteric enzymes.
  • Understanding allosteric mechanisms is critical for enzyme engineering and drug development.