Title
Compaction properties of an intrinsically disordered protein : sic1 and its kinase-inhibitor domain
Author
Faculty/Department
Faculty of Sciences. Chemistry
Publication type
article
Publication
New York, N.Y. ,
Subject
Physics
Biology
Source (journal)
Biophysical journal. - New York, N.Y.
Volume/pages
100(2011) :9 , p. 2243-2252
ISSN
0006-3495
ISI
000290360000022
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
IDPs in their unbound state can transiently acquire secondary and tertiary structure. Describing such intrinsic structure is important to understand the transition between free and bound state, leading to supramolecular complexes with physiological interactors. IDP structure is highly dynamic and, therefore, difficult to study by conventional techniques. This work focuses on conformational analysis of the KID fragment of the Sic1 protein, an IDP with a key regulatory role in the cell-cycle of Saccharomyces cerevisiae. FT-IR spectroscopy, ESI-MS, and IM measurements are used to capture dynamic and short-lived conformational states, probing both secondary and tertiary protein structure. The results indicate that the isolated Sic1 KID retains dynamic helical structure and populates collapsed states of different compactness. A metastable, highly compact species is detected. Comparison between the fragment and the full-length protein suggests that chain length is crucial to the stabilization of compact states of this IDP. The two proteins are compared by a length-independent compaction index.
Full text (open access)
https://repository.uantwerpen.be/docman/irua/bd9e2d/5013.pdf
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