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Proceedings Paper

Study conformational dynamics of intrinsically disordered protein by PET-FCS (Conference Presentation)
Author(s): Joerg Enderlein; Man Zhou; Qui Van; Ingo Gregor

Paper Abstract

Intrinsically disordered proteins (IDP) form a large and functionally important class of proteins that lack an ordered three-dimensional structure. IDPs play an important role in cell signaling, transcription, or chromatin remodeling. The discovery of IDPs has challenged the traditional paradigm of protein structure which states that protein function depends on a well-defined three-dimensional structure. Due to their high conformational flexibility and the lack of ordered secondary structure, it is challenging to study the flexible structure, dynamics and energetics of these proteins with conventional methods. In our work, we employ photoinduced electron transfer (PET) combined with fluorescence correlation spectroscopy (FCS) for studying the conformational dynamics of one specific class of IDPs: phenylalanine-glycine rich protein domains (FG repeats) which are dominant building blocks within the pore of nuclear pore complexes. Nuclear pore complexes are large protein assemblies that cross the nuclear envelope and form selective barrier, which regulate bidirectional exchange between nucleus and cytoplasm.

Paper Details

Date Published: 27 April 2016
PDF: 1 pages
Proc. SPIE 9714, Single Molecule Spectroscopy and Superresolution Imaging IX, 971404 (27 April 2016); doi: 10.1117/12.2212247
Show Author Affiliations
Joerg Enderlein, Georg-August-Univ. Göttingen (Germany)
Man Zhou, Georg-August-Univ. Göttingen (Germany)
Qui Van, Georg-August-Univ. Göttingen (Germany)
Ingo Gregor, Georg-August-Univ. Göttingen (Germany)


Published in SPIE Proceedings Vol. 9714:
Single Molecule Spectroscopy and Superresolution Imaging IX
Jörg Enderlein; Ingo Gregor; Zygmunt Karol Gryczynski; Rainer Erdmann; Felix Koberling, Editor(s)

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