Fuzziness enables context dependence of protein interactions

Marton Miskei, Andrea Gregus, Rashmi Sharma, Norbert Duro, Fruzsina Zsolyomi, Monika Fuxreiter

Research output: Contribution to journalReview article

21 Citations (Scopus)


Proteins may undergo adaptive structural transitions to accommodate to their cellular milieu and respond to external signals. Modulation of conformational ensembles can rewire the intra- or intermolecular interaction networks and shift between different functional states. Adaptive conformational transitions are associated with protein fuzziness, which enables (a) rewiring interaction networks via alternative motifs, (b) new functional features via allosteric motifs, (c) functional switches upon post-translational modifications, or (d) regulation of higher-order organizations. We propose that all these context-dependent functional changes are intertwined with structural multiplicity or dynamic disorder in protein assemblies and can only be described by stochastic structure–function relationships.

Original languageEnglish
Pages (from-to)2682-2695
Number of pages14
JournalFEBS letters
Issue number17
Publication statusPublished - Sep 2017


  • fuzzy complex
  • intrinsically disordered proteins
  • protein interactions

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Fuzziness enables context dependence of protein interactions'. Together they form a unique fingerprint.

  • Cite this

    Miskei, M., Gregus, A., Sharma, R., Duro, N., Zsolyomi, F., & Fuxreiter, M. (2017). Fuzziness enables context dependence of protein interactions. FEBS letters, 591(17), 2682-2695. https://doi.org/10.1002/1873-3468.12762