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Related Concept Videos

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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Molecular Weight of Step-Growth Polymers01:08

Molecular Weight of Step-Growth Polymers

Step growth polymerization involves bi or multifunctional monomers. Bifunctional monomers react to form linear step growth polymers, whereas multifunctional monomers react to form non-linear or branched polymers.
As the step-growth polymerization involves step-wise condensation of monomers, the molecular weight also builds up eventually. Consequently, high molecular weight polymers are obtained at the late stages of the polymerization, where 99% of monomers have been consumed.
The extent of the...

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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Dynamic oligomeric properties.

Norbert W Seidler1

  • 1Department of Biochemistry, Kansas City University of Medicine and Biosciences, Kansas City, MO, USA.

Advances in Experimental Medicine and Biology
|August 2, 2012
PubMed
Summary
This summary is machine-generated.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) oligomerization is key to its function. Factors like substrates, coenzymes, and ions influence its stability and dynamic equilibrium, revealing insights into protein regulation.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Protein oligomerization is a crucial strategy for stabilizing protein conformation and function.
  • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) exhibits dynamic oligomeric properties influencing its functional diversity.
  • Understanding these properties is vital for comprehending enzyme regulation and cellular processes.

Purpose of the Study:

  • To explore the relationship between dynamic oligomeric states and functional diversity of GAPDH.
  • To analyze the structural basis of GAPDH conformational sub-states and protein stability.
  • To investigate factors affecting GAPDH oligomerization and regulation.

Main Methods:

  • Discussion of structural basis for conformational sub-states.
  • Analysis of protein stability factors.
  • Examination of effects of chemical modifications, substrates, coenzymes, and ions on oligomerization.
  • Comparative analyses across diverse species.
  • Introduction of domain exchange concept.

Main Results:

  • Chloride ions exhibit a destabilizing effect on native GAPDH structure.
  • Adenine dinucleotides play a significant role in regulating tetramer-dimer equilibrium dynamics.
  • Comparative analyses offer insights into protein stability and subunit interactions.
  • Domain exchange is proposed as a mechanism for stabilizing dynamic oligomers.

Conclusions:

  • GAPDH oligomerization dynamics, influenced by various factors, are central to its physiological regulation.
  • Inter-subunit contacts can modulate protein interactions by masking docking sites.
  • Further research into dynamic oligomeric properties can uncover novel functional mechanisms.