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Related Concept Videos

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.
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Protein Complexes with Interchangeable Parts01:57

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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A polymetamorphic protein.

Katie L Stewart1, Eric D Dodds, Vicki H Wysocki

  • 1Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, USA.

Protein Science : a Publication of the Protein Society
|March 9, 2013
PubMed
Summary
This summary is machine-generated.

Introducing hydrophobic mutations into Arc repressor protein progressively reduces fold specificity. This leads to altered native folds, changes in fold coupled to oligomerization, and a continuum of protein structures.

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Area of Science:

  • Protein structure and folding
  • Biophysics
  • Molecular biology

Background:

  • Arc repressor is a homodimeric protein with a ribbon-helix-helix fold.
  • A single mutation (N11L) alters its dimeric fold, replacing a β-sheet with 3₁₀ helices.

Purpose of the Study:

  • To investigate the effects of accumulating hydrophobic mutations on Arc repressor's fold specificity and oligomerization.
  • To characterize the structural properties of a variant with multiple surface mutations (Q9V/N11L/R13V, S-VLV).

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to compare protein topologies.
  • Analysis of protein structure and oligomerization states.

Main Results:

  • The S-VLV variant forms a stable, reversibly folded octamer with reduced α-helical content compared to wild-type Arc.
  • At low concentrations and ionic strength, S-VLV populates multiple dimeric topologies.
  • Increased hydrophobicity in Arc variants leads to reduced fold specificity and a range of structures, from dimers to octamers.

Conclusions:

  • Accumulating hydrophobic mutations in Arc repressor progressively destabilizes its native fold, leading to altered native folds, changes in fold coupled to oligomerization, and a continuum of accessible protein structures.
  • While a hydrophobic stretch in S-VLV is predicted to be amyloidogenic, aggregation is limited to octamers, suggesting complex effects of hydrophobicity on protein structure space.