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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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...
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Allosteric Proteins-ATCase01:19

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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...
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X-ray Crystallography02:18

X-ray Crystallography

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The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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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...
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Crystal Field Theory - Octahedral Complexes02:58

Crystal Field Theory - Octahedral Complexes

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Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...
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X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

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X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal...
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Related Experiment Video

Updated: Jun 6, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Exploring the dynamics of allostery through multi-dimensional crystallography.

C E Hatton1, P Mehrabi1,2

  • 1Institute for Nanostructure and Solid-State Physics, University of Hamburg, Hamburg, Germany.

Biophysical Reviews
|December 2, 2024
PubMed
Summary

This review explores multi-dimensional crystallography to understand how allosteric proteins change with time and temperature. These advanced structural biology methods reveal crucial links between protein structure, dynamics, and function.

Keywords:
AllosteryEnzymesTemperatureTime-resolved crystallography

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Area of Science:

  • Structural biology
  • Biophysics
  • Molecular biology

Background:

  • Allosteric proteins are crucial regulators of cellular processes.
  • Understanding allosteric mechanisms requires insights into protein dynamics.
  • Traditional crystallography often captures static protein structures.

Purpose of the Study:

  • To review applications and methodologies of multi-dimensional crystallography.
  • To elucidate the structure-dynamics-function relationship in allosteric proteins.
  • To highlight the role of time and temperature variations in studying allostery.

Main Methods:

  • Multi-dimensional crystallography (time-resolved and temperature-dependent).
  • Analysis of case studies involving allosteric proteins.
  • Integration of structural data with dynamic information.

Main Results:

  • Demonstrates how varying time and temperature reveals dynamic allosteric mechanisms.
  • Provides insights into the conformational changes of allosteric proteins.
  • Highlights the power of multi-dimensional approaches in structural biology.

Conclusions:

  • Multi-dimensional crystallography is essential for deciphering allosteric mechanisms.
  • Integrating time and temperature provides a dynamic view of protein function.
  • This approach opens new frontiers in understanding the molecular basis of life.