Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins

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The physics and bioinformatics of binding and folding—an energy landscape perspective

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Intrinsic disorder in cell signaling and gene transcription

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Proteins with weakly funneled energy landscapes challenge the classical structure–function paradigm

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Electrostatically Accelerated Coupled Binding and Folding of Intrinsically Disordered Proteins

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On the Importance of Polar Interactions for Complexes Containing Intrinsically Disordered Proteins

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Energetic Basis of Uncoupling Folding from Binding for an Intrinsically Disordered Protein

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NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1

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Incorporating 1H chemical shift determination into 13C-direct detected spectroscopy of intrinsically disordered proteins in solution

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Carbon-Detected 15N NMR Spin Relaxation of an Intrinsically Disordered Protein: FCP1 Dynamics Unbound and in Complex with RAP74

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The disordered C-terminus of the RNA Polymerase II phosphatase FCP1 is partially helical in the unbound state

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Atomistic Simulations Reveal Structural Disorder in the RAP74-FCP1 Complex

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Thermodynamics of Coupled Folding in the Interaction of Archaeal RNase P Proteins RPP21 and RPP29

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Native-Based Simulations of the Binding Interaction Between RAP74 and the Disordered FCP1 Peptide

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NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state

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Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation

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Cold stability of intrinsically disordered proteins

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How disorder influences order and vice versa – mutual effects in fusion proteins containing an intrinsically disordered and a globular protein

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Templated folding of intrinsically disordered proteins

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