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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 10: Towards Understanding Protein Disorder In-Cell
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Chapter title
Towards Understanding Protein Disorder In-Cell
Chapter number 10
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_10
Pubmed ID
Book ISBNs
978-3-31-920163-4, 978-3-31-920164-1
Authors

Cesyen Cedeño, Hadas Raveh-Hamit, András Dinnyés, Peter Tompa, Cedeño, Cesyen, Raveh-Hamit, Hadas, Dinnyés, András, Tompa, Peter

Abstract

Investigating the activity and structure of cellular biochemical machinery at atomic resolution has been a point of paramount significance for understanding health and disease over the decades. The underlying molecular mechanisms are primarily studied in vitro. Nuclear magnetic resonance (NMR) is a technique that allows to look into cells and study proteins and other constituents, thanks to careful experimental design and technological advances (spectrometer sensitivity and pulse sequence design). Here we outline current applications of the technique and propose a realistic future for the field.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 7 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 7 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 1 14%
Professor > Associate Professor 1 14%
Lecturer > Senior Lecturer 1 14%
Student > Master 1 14%
Unknown 3 43%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 2 29%
Agricultural and Biological Sciences 1 14%
Unknown 4 57%