Premium
Electrospray ionization‐mass spectrometry conformational analysis of isolated domains of an intrinsically disordered protein
Author(s) -
Testa Lorenzo,
Brocca Stefania,
Šamalikova Maria,
Santambrogio Carlo,
Alberghina Lilia,
Grandori Rita
Publication year - 2011
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.201000253
Subject(s) - electrospray ionization , mass spectrometry , chemistry , intrinsically disordered proteins , electrospray , conformational change , biophysics , chromatography , biochemistry , biology
The highly dynamic and heterogeneous molecular ensembles characterizing intrinsically disordered proteins (IDP) in solution pose major challenges to the conventional methods for structural analysis. Electrospray ionization‐mass spectrometry (ESI‐MS) allows direct detection of distinct conformational components, effectively capturing also partially folded and short‐lived states. We report the description of two complementary fragments (1–186 and 187–284) of the IDP Sic1, a cyclin‐dependent protein kinase inhibitor of yeast Saccharomyces cerevisiae . Structural heterogeneity is noted in both cases, but the two fragments reveal slightly different conformational properties. The results are consistent with previously reported differences between the two protein moieties and corroborate the feasibility of IDP conformational analysis by ESI‐MS.