Related Experiment Video
Updated: Jun 6, 2026
09:25
NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Protein dynamics and allostery: an NMR view
Shiou-Ru Tzeng1, Charalampos G Kalodimos
1Department of Chemistry & Chemical Biology, Rutgers University, Piscataway, NJ 08854, USA.
Current Opinion in Structural Biology
|November 27, 2010
Summary
Allostery regulation involves protein dynamics, not just structure. Protein motions and conformational entropy are key to allosteric interactions and ligand binding, challenging classical views.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Dynamics
Background:
- Allostery is a fundamental mechanism for protein activity regulation through energetically coupled distant sites.
- The classical view of allostery primarily emphasizes structural changes.
- Emerging evidence highlights the critical role of internal protein motions in allosteric regulation.
Purpose of the Study:
- To discuss the emerging paradigms of allostery, focusing on the central role of protein dynamics.
- To illustrate the link between protein internal motions and function in protein-ligand interactions.
- To present a broader understanding of allosteric mechanisms beyond purely structural changes.
Main Methods:
- Review and synthesis of recent examples and research findings.
- Analysis of the interplay between protein dynamics, conformational states, and ligand binding.
- Discussion of the role of conformational entropy in allosteric energy transfer.
Main Results:
- Proteins actively redistribute their motions in response to perturbations.
- Fluctuating conformational states and protein dynamics are crucial for ligand binding.
- Allosteric interactions can occur with minimal or no significant structural changes, driven by dynamics.
Conclusions:
- Protein dynamics, including internal motions and conformational entropy, are integral to allostery.
- A dynamic view of allostery complements and expands upon the classical structural perspective.
- Understanding protein dynamics is essential for comprehending allosteric regulation and function.
Related Concept Videos
01:58Cooperative 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...
01:58Cooperative 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...
01:58Cooperative 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...
01:19Protein Dynamics in Living Cells
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
01:19Allosteric 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,...
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,...
00:52¹H 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...