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

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0065-2598 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.978-3-319-37117-7978-3-319-20164-1Series ISSN 0065-2598 Series E-ISSN 2214-8019

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https://doi.org/10.1007/978-3-319-20164-1NMR spectroscopy; bioinformatics; functional IDP regions; intrinsically disordered proteins; nuclear mag

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978-3-319-37117-7The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Nature Switzerl

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Structure and Dynamics of Intrinsically Disordered Proteins,tion. We are only beginning, however, to develop a detailed knowledge of the structure and dynamics of these proteins. It is becoming increasingly clear that, as IDPs populate highly heterogeneous states, they should be described in terms of conformational ensembles rather than as individual structu

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NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactioor atomic resolution characterization of intrinsically disordered proteins (IDPs) that are optimized for the particular chemical and spectroscopic properties of these molecules. A wide range of NMR observables can now be measured on increasingly complex IDPs that report on their structural and dynam

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Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters,erved in IDPs, commonly described as transient/dynamic or expressed in terms of fractional populations. In order to understand how the protein primary sequence dictates the dynamic and structural properties of IDPs and in general to understand how IDPs function, atomic-level descriptions are needed.