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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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The entropic force generated by intrinsically disordered segments tunes protein function.

Nicholas D Keul1, Krishnadev Oruganty2, Elizabeth T Schaper Bergman3

  • 1Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.

Nature
|November 14, 2018
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered peptide segments can enhance protein function by shifting conformational ensembles. This entropic effect, driven by the length of disordered regions, optimizes inhibitor binding in UDP-α-D-glucose-6-dehydrogenase (UGDH).

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Protein structures are dynamic, exploring various conformations crucial for function.
  • The role of intrinsically disordered regions in protein evolution and function is not well understood.
  • A significant portion of the human proteome contains intrinsically disordered segments with unknown functions.

Purpose of the Study:

  • To investigate how intrinsically disordered peptide segments influence protein conformational ensembles and function.
  • To determine the mechanism by which intrinsically disordered carboxy-termini affect protein-ligand interactions.
  • To explore the evolutionary implications of intrinsically disordered segments in protein adaptation.

Main Methods:

  • Studied the human UDP-α-D-glucose-6-dehydrogenase (UGDH) protein.
  • Investigated the effect of an intrinsically disordered carboxy-terminal tail (ID-tail) on UGDH's conformational ensemble.
  • Analyzed the relationship between ID-tail length and affinity for an allosteric inhibitor.

Main Results:

  • The ID-tail shifts the UGDH conformational ensemble towards a state with higher affinity for an allosteric inhibitor.
  • The observed affinity enhancement is dependent on the length of the intrinsically disordered segment, not its sequence or composition.
  • This effect is consistent with the entropic force generated by an unstructured peptide.

Conclusions:

  • The intrinsically disordered tail acts as an 'entropic rectifier,' favoring inhibitor binding by modulating protein dynamics and structure.
  • This mechanism provides an easily acquired adaptation, suggesting evolution may select for disordered segments to tune protein energy landscapes.
  • The findings offer a potential explanation for the prevalence of intrinsic disorder in the proteome.