Titlebook: Intrinsically Disordered Proteins Studied by NMR Spectroscopy; Isabella C. Felli,Roberta Pierattelli Book 2015 The Editor(s) (if applicabl

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Jenny Erales,David Blocquel,Johnny Habchi,Matilde Beltrandi,Antoine Gruet,Marion Dosnon,Christophe Brklärt, sondern auch solche die in zukünftigen Pkw- und Bahnantrieben zum Einsatz kommen werden, wie z.B. Reluktanz- und Transversalflussmotor. Im letzen Kapitel werden Antriebssysteme am Beispiel einer E-Lok und der Magnetschwebebahn, auch supraleitender MAGLEV, vorgestellt.978-3-8348-9150-1

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Intrinsically Disordered Proteins Studied by NMR Spectroscopy

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Book 2015properties, computational methods to describe the structure and dynamics are in continuous development and IDPs can be studied in environments as complex as whole cells. This volume communicates the new exciting possibilities offered by NMR and presents open questions to foster further developments.

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NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and InteractioMR studies of IDPs (Sect. 3.3), 2D HN and CON NMR experiments: the fingerprint of an IDP (Sect. 3.4), tools for overcoming major bottlenecks of IDP NMR studies (Sect. 3.5), .C detected experiments (Sect. 3.6), from 2D to 3D: from simple snapshots to site-resolved characterization of IDPs (Sect. 3.7)

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NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins,ciation processes frequently occur on time scales that are amenable to NMR spectroscopy we describe in detail the application of CPMG relaxation dispersion techniques to studies of IDP protein binding. Finally, we demonstrate that the complementary usage of NMR and EPR data provide a more comprehens

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Application of SAXS for the Structural Characterization of IDPs,nd intrinsically disordered proteins (IDPs). A major recent development is the use of SAXS to study particle dynamics in solution by ensemble approaches, which allow one to quantitatively characterize flexible systems. Of special interest is the joint use of SAXS with solution NMR, given that both m

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Bioinformatics Approaches for Predicting Disordered Protein Motifs,units that confer versatility to protein function and SLiM-mediated interactions are increasingly being recognized as therapeutic targets. In this chapter we start with a brief description about the properties of SLiMs and their interactions and then move on to discuss algorithms and tools including

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The Protein Ensemble Database,quences of inherent flexibility. The Protein Ensemble Database (http://pedb.vib.be) is the first openly accessible, manually curated online resource storing the ensemble models, protocols used during the calculation procedure, and underlying primary experimental data derived from SAXS and/or NMR mea

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