Electrospray ionization-mass spectrometry conformational analysis of isolated domains of an intrinsically disordered protein

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...

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Bibliographic Details
Published in:Biotechnology journal 2011-01, Vol.6 (1), p.96-100
Main Authors: Testa, Lorenzo, Brocca, Stefania, Šamalikova, Maria, Santambrogio, Carlo, Alberghina, Lilia, Grandori, Rita
Format: Article
Language:English
Subjects:
Charge state distributions
Cyclin-Dependent Kinase Inhibitor Proteins - chemistry
Cyclin-dependent protein kinase inhibitors
Nano-electrospray
Partially folded states
Protein Conformation
Protein Structure, Tertiary
Proteins - chemistry
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins - chemistry
Sic1
Spectrometry, Mass, Electrospray Ionization - methods
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Summary: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.
ISSN:1860-6768
1860-7314
1860-7314
DOI:10.1002/biot.201000253