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Titlebook: Intrinsically Disordered Protein Analysis; Volume 2, Methods an Vladimir N. Uversky,A. Keith Dunker Book 2012 Springer Science+Business Med

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Identification of Intrinsically Disordered Proteins by a Special 2D Electrophoresisheat-treated proteins where IDPs are expected to run into the diagonal of the gel, whereas globular proteins either precipitate upon heat treatment or unfold and run off the diagonal in the second dimension.
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Analysis of Intrinsically Disordered Proteins by Small-Angle X-ray Scatteringns are given and the sequence of steps in data collection and processing is described. The use of the recently developed advanced computational tools to quantitatively characterize solutions of IDPs is presented in detail. Typical experimental and potential problems encountered during the use of SAXS are discussed.
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pH-Induced Changes in Intrinsically Disordered Proteinstructure under highly acidic or basic conditions. Here, we describe circular dichroism and fluorescence spectroscopic experimental approaches in which the conformation of proteins is monitored as pH is altered as a way of testing whether the protein behaves as an intrinsically disordered protein.
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Visualization of Mobility by Atomic Force Microscopyred protein (IDP) and show undulation motion of the IDRs. The visualized tail-like structures contain the information of mechanical properties of the IDRs. Here, we describe methods of HS-AFM visualization of IDPs and methods of analyzing the obtained images to characterize IDRs.
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Sedimentation Velocity Analytical Ultracentrifugation for Intrinsically Disordered Proteinso and can be easily interpreted in terms of frictional ratio. This chapter is a step-by-step protocol for setting up, executing and analyzing SV experiments in the context of the characterization of IDPs, based on a real case study of the partially folded C-terminal domain of Sendai virus nucleoprotein.
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