Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin.
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ABSTRACT:
SUBMITTER: Kurzbach D
PROVIDER: S-EPMC3737600 | biostudies-literature | 2013 Aug
REPOSITORIES: biostudies-literature
Publications
Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin.
Kurzbach Dennis D Platzer Gerald G Schwarz Thomas C TC Henen Morkos A MA Konrat Robert R Hinderberger Dariush D
Biochemistry 20130724 31
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 demons ...[more]
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