Physical Background of the Disordered Nature of "Mutual Synergetic Folding" Proteins

C. Magyar, Anikó Mentes, Erzsébet Fichó, Miklós Cserző, I. Simon

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Intrinsically disordered proteins (IDPs) lack a well-defined 3D structure. Their disordered nature enables them to interact with several other proteins and to fulfil their vital biological roles, in most cases after coupled folding and binding. In this paper, we analyze IDPs involved in a new mechanism, mutual synergistic folding (MSF). These proteins define a new subset of IDPs. Recently we collected information on these complexes and created the Mutual Folding Induced by Binding (MFIB) database. These protein complexes exhibit considerable structural variation, and almost half of them are homodimers, but there is a significant amount of heterodimers and various kinds of oligomers. In order to understand the basic background of the disordered character of the monomers found in MSF complexes, the simplest part of the MFIB database, the homodimers are analyzed here. We conclude that MFIB homodimeric proteins have a larger solvent-accessible main-chain surface area on the contact surface of the subunits, when compared to globular homodimeric proteins. The main driving force of the dimerization is the mutual shielding of the water-accessible backbones and the formation of extra intermolecular interactions.

Original languageEnglish
JournalInternational Journal of Molecular Sciences
Volume19
Issue number11
DOIs
Publication statusPublished - Oct 26 2018

Fingerprint

Protein folding
Protein Folding
Intrinsically Disordered Proteins
folding
proteins
Proteins
Databases
Dimerization
Oligomers
Shielding
Carrier Proteins
Monomers
Water
dimerization
oligomers
set theory
shielding
monomers

Keywords

  • dehydron
  • homodimer
  • hydrogen bond
  • inter-subunit interaction
  • intrinsically disordered protein
  • ion pair
  • mutual synergistic folding
  • solvent-accessible surface area
  • stabilization center

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

Cite this

Physical Background of the Disordered Nature of "Mutual Synergetic Folding" Proteins. / Magyar, C.; Mentes, Anikó; Fichó, Erzsébet; Cserző, Miklós; Simon, I.

In: International Journal of Molecular Sciences, Vol. 19, No. 11, 26.10.2018.

Research output: Contribution to journalArticle

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