Journal
BIOCHEMISTRY
Volume 52, Issue 31, Pages 5167-5175Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi400502c
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [HI 1094/2-1]
- Max Planck Graduate Center
- University of Mainz (MPGC)
- Austrian Science Fund (FWF) [P20549-N19, P22125-B12, W1221]
- Forschungsstipendium
- OAD
- Gutenberg Academy of the University of Mainz
- Austrian Science Fund (FWF) [P20549] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [P 20549] Funding Source: researchfish
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Intrinsically disordered proteins (IDPs) constitute a class of biologically active proteins that lack defined tertiary and often secondary structure. The IDP Osteopontin (OPN), a cytokine involved in metastasis of several types of cancer, is shown to simultaneously sample extended, random coil-like conformations and stable, cooperatively folded conformations. By a combination of two magnetic resonance methods, electron paramagnetic resonance and nuclear magnetic resonance spectroscopy, we demonstrate that the OPN ensemble exhibits not only characteristics of an extended and flexible polypeptide, as expected for an IDP, but also simultaneously those of globular proteins, in particular sigmoidal structural denaturation profiles. Both types of states, extended and cooperatively folded, are populated simultaneously by OPN in its apo state. The heterogeneity of the structural properties of IDPs is thus shown to even involve cooperative folding and unfolding events.
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