Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study

Eszter Németh, Ria K. Balogh, Katalin Borsos, Anikó Czene, Peter W. Thulstrup, Béla Gyurcsik

Research output: Article

3 Citations (Scopus)


X-ray diffractometry dominates protein studies, as it can provide 3D structures of these diverse macromolecules or their molecular complexes with interacting partners: substrates, inhibitors, and/or cofactors. Here, we show that under cocrystallization conditions the results could reflect induced protein folds instead of the (partially) disordered original structures. The analysis of synchrotron radiation circular dichroism spectra revealed that the Im7 immunity protein stabilizes the native-like solution structure of unfolded NColE7 nuclease mutants via complex formation. This is consistent with the fact that among the several available crystal structures with its inhibitor or substrate, all NColE7 structures are virtually the same. Our results draw attention to the possible structural consequence of protein modifications, which is often hidden by compensational effects of intermolecular interactions. The growing evidence on the importance of protein intrinsic disorder thus, demands more extensive complementary experiments in solution phase with the unligated form of the protein of interest.

Original languageEnglish
Pages (from-to)1977-1988
Number of pages12
JournalProtein Science
Issue number11
Publication statusPublished - nov. 1 2016

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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