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Intrinsically Disordered Protein Analysis

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Cover of 'Intrinsically Disordered Protein Analysis'

Table of Contents

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    Book Overview
  2. Altmetric Badge
    Chapter 1 Determination of IUP Based on Susceptibility for Degradation by Default
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    Chapter 2 In-cell NMR of intrinsically disordered proteins in prokaryotic cells.
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    Chapter 3 In-Cell NMR in Xenopus laevis Oocytes.
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    Chapter 4 In-cell NMR in Mammalian cells: part 1.
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    Chapter 5 In-cell NMR in Mammalian cells: part 2.
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    Chapter 6 In-cell NMR in Mammalian cells: part 3.
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    Chapter 7 Fourier Transform Infrared Microspectroscopy of Complex Biological Systems: From Intact Cells to Whole Organisms
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    Chapter 8 Studying IDP Stability and Dynamics by Fast Relaxation Imaging in Living Cells
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    Chapter 9 Measurement and Analysis of NMR Residual Dipolar Couplings for the Study of Intrinsically Disordered Proteins
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    Chapter 10 Distance Information for Disordered Proteins from NMR and ESR Measurements Using Paramagnetic Spin Labels
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    Chapter 11 Using Chemical Shifts to Assess Transient Secondary Structure and Generate Ensemble Structures of Intrinsically Disordered Proteins
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    Chapter 12 Magic Angle Spinning Solid-State NMR Experiments for Structural Characterization of Proteins
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    Chapter 13 Wide-Line NMR and Protein Hydration
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    Chapter 14 5-Fluoro- d,l -Tryptophan as a Dual NMR and Fluorescent Probe of α-Synuclein
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    Chapter 15 Alpha Proton Detection Based Backbone Assignment of Intrinsically Disordered Proteins
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    Chapter 16 Fourier Transform Infrared Spectroscopy of Intrinsically Disordered Proteins: Measurement Procedures and Data Analyses
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    Chapter 17 Monitoring Structural Transitions in IDPs by Vibrational Spectroscopy of Cyanylated Cysteine.
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    Chapter 18 Structure Analysis of Unfolded Peptides I: Vibrational Circular Dichroism Spectroscopy
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    Chapter 19 Structural Analysis of Unfolded Peptides by Raman Spectroscopy
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    Chapter 20 Isotope-Edited Infrared Spectroscopy
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    Chapter 21 Monitoring Structural Transitions in IDPs by Site-Directed Spin Labeling EPR Spectroscopy.
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    Chapter 22 Circular Dichroism Techniques for the Analysis of Intrinsically Disordered Proteins and Domains
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    Chapter 23 Deconstructing Time-Resolved Optical Rotatory Dispersion Kinetic Measurements of Cytochrome c Folding: From Molten Globule to the Native State
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    Chapter 24 The Use of UV–Vis Absorption Spectroscopy for Studies of Natively Disordered Proteins
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    Chapter 25 Intrinsic Fluorescence of Intrinsically Disordered Proteins
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    Chapter 26 Binding Stoichiometry and Affinity of Fluorescent Dyes to Proteins in Different Structural States
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    Chapter 27 Fluorescence Lifetime Measurements of Intrinsically Unstructured Proteins: Application to α-Synuclein
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    Chapter 28 Ensemble FRET Methods in Studies of Intrinsically Disordered Proteins
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    Chapter 29 Fluorescence Correlation Spectroscopy to Determine the Diffusion Coefficient of α-Synuclein and Follow Early Oligomer Formation
Attention for Chapter 3: In-Cell NMR in Xenopus laevis Oocytes.
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Chapter title
In-Cell NMR in Xenopus laevis Oocytes.
Chapter number 3
Book title
Intrinsically Disordered Protein Analysis
Published in
Methods in molecular biology, July 2012
DOI 10.1007/978-1-61779-927-3_3
Pubmed ID
Book ISBNs
978-1-61779-926-6, 978-1-61779-927-3
Authors

Thongwichian R, Selenko P, Rossukon Thongwichian, Philipp Selenko

Abstract

For the purpose of studying IDPs inside cells of higher organisms, several eukaryotic in-cell NMR systems have been developed over the past years. In this chapter we will focus on high-resolution in-cell NMR applications in Xenopus laevis oocytes, the first eukaryotic cellular model system to be established. In contrast to prokaryotic in-cell NMR samples, eukaryotic in-cell NMR specimens are prepared by cytoplasmic delivery of an exogenously produced, isotope-labeled protein into the non-isotope-labeled environment of the respective "host" cell. In-cell NMR applications in Xenopus oocytes rely on intracellular sample deposition by direct microinjection into the oocyte cytoplasm. Here, we describe the preparation of oocyte in-cell NMR samples for IDP studies in this cellular model environment.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 21 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Japan 1 5%
United States 1 5%
Unknown 19 90%

Demographic breakdown

Readers by professional status Count As %
Researcher 8 38%
Student > Ph. D. Student 3 14%
Student > Bachelor 2 10%
Student > Postgraduate 2 10%
Student > Doctoral Student 1 5%
Other 4 19%
Unknown 1 5%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 9 43%
Agricultural and Biological Sciences 6 29%
Chemistry 4 19%
Arts and Humanities 1 5%
Unknown 1 5%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 18 December 2012.
All research outputs
#15,258,711
of 22,689,790 outputs
Outputs from Methods in molecular biology
#5,294
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Outputs of similar age
#104,905
of 164,312 outputs
Outputs of similar age from Methods in molecular biology
#17
of 52 outputs
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