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Intrinsically Disordered Proteins Studied by NMR Spectroscopy

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Cover of 'Intrinsically Disordered Proteins Studied by NMR Spectroscopy'

Table of Contents

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    Book Overview
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    Chapter 1 Back to the Future: Nuclear Magnetic Resonance and Bioinformatics Studies on Intrinsically Disordered Proteins.
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    Chapter 2 Structure and Dynamics of Intrinsically Disordered Proteins.
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    Chapter 3 NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines
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    Chapter 4 Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters
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    Chapter 5 NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins.
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    Chapter 6 Recombinant Intrinsically Disordered Proteins for NMR: Tips and Tricks.
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    Chapter 7 Biophysical Methods to Investigate Intrinsically Disordered Proteins: Avoiding an "Elephant and Blind Men" Situation.
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    Chapter 8 Application of SAXS for the Structural Characterization of IDPs
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    Chapter 9 Bioinformatics Approaches for Predicting Disordered Protein Motifs
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    Chapter 10 Towards Understanding Protein Disorder In-Cell
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    Chapter 11 The Protein Ensemble Database
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    Chapter 12 Order and Disorder in the Replicative Complex of Paramyxoviruses.
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    Chapter 13 Druggability of Intrinsically Disordered Proteins.
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    Chapter 14 Beta Amyloid Hallmarks: From Intrinsically Disordered Proteins to Alzheimer's Disease.
Attention for Chapter 4: Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters
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Chapter title
Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters
Chapter number 4
Book title
Intrinsically Disordered Proteins Studied by NMR Spectroscopy
Published in
Advances in experimental medicine and biology, January 2015
DOI 10.1007/978-3-319-20164-1_4
Pubmed ID
Book ISBNs
978-3-31-920163-4, 978-3-31-920164-1
Authors

Jaka Kragelj, Martin Blackledge, Malene Ringkjøbing Jensen, Kragelj, Jaka, Blackledge, Martin, Jensen, Malene Ringkjøbing

Abstract

Intrinsically disordered proteins (IDPs) perform their function despite their lack of well-defined tertiary structure. Residual structure has been observed 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. Nuclear magnetic resonance spectroscopy provides information about local and long-range structure in IDPs at amino acid specific resolution and can be used in combination with ensemble descriptions to represent the dynamic nature of IDPs. In this chapter we describe sample-and-select approaches for ensemble modelling of local structural propensities in IDPs with specific emphasis on validation of these ensembles.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 28 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 28 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 12 43%
Professor 3 11%
Student > Ph. D. Student 2 7%
Other 1 4%
Librarian 1 4%
Other 2 7%
Unknown 7 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 29%
Chemistry 5 18%
Agricultural and Biological Sciences 4 14%
Materials Science 1 4%
Unknown 10 36%