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Heterologous Expression of Membrane Proteins

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Cover of 'Heterologous Expression of Membrane Proteins'

Table of Contents

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    Book Overview
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    Chapter 1 Heterologous Expression of Membrane Proteins
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    Chapter 2 Heterologous Expression of Membrane Proteins
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    Chapter 3 Membrane Protein Production in Escherichia coli: Protocols and Rules.
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    Chapter 4 Codon Optimizing for Increased Membrane Protein Production: A Minimalist Approach.
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    Chapter 5 Generation of Tetracycline-Inducible Mammalian Cell Lines by Flow Cytometry for Improved Overproduction of Membrane Proteins.
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    Chapter 6 Membrane Protein Production in Lactococcus lactis for Functional Studies.
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    Chapter 7 Heterologous Expression of Membrane Proteins
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    Chapter 8 Leishmania tarentolae as a Promising Tool for Expressing Polytopic and Multi-Transmembrane Spans Eukaryotic Membrane Proteins: The Case of the ABC Pump ABCG6.
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    Chapter 9 Overexpression, Membrane Preparation, and Purification of a Typical Multidrug ABC Transporter BmrA.
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    Chapter 10 Heterologous Expression of Membrane Proteins
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    Chapter 11 Heterologous Expression of Membrane Proteins
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    Chapter 12 Heterologous Expression of Membrane Proteins
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    Chapter 13 Heterologous Expression of Membrane Proteins
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    Chapter 14 Heterologous Expression of Membrane Proteins
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    Chapter 15 Membrane Protein Solubilization and Composition of Protein Detergent Complexes.
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    Chapter 16 Detergent-Free Membrane Protein Purification.
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    Chapter 17 Conformational Dynamics and Interactions of Membrane Proteins by Hydrogen/Deuterium Mass Spectrometry.
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    Chapter 18 Lessons from an α-Helical Membrane Enzyme: Expression, Purification, and Detergent Optimization for Biophysical and Structural Characterization.
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    Chapter 19 Heterologous Expression of Membrane Proteins
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Chapter title
Heterologous Expression of Membrane Proteins
Chapter number 10
Book title
Heterologous Expression of Membrane Proteins
Published in
Methods in molecular biology, January 2016
DOI 10.1007/978-1-4939-3637-3_10
Pubmed ID
Book ISBNs
978-1-4939-3635-9, 978-1-4939-3637-3
Authors

Hartmann, Lucie, Kugler, Valérie, Wagner, Renaud, Lucie Hartmann, Valérie Kugler, Renaud Wagner

Editors

Isabelle Mus-Veteau

Abstract

A key point when it comes to heterologous expression of eukaryotic membrane proteins (EMPs) is the choice of the best-suited expression platform. The yeast Pichia pastoris has proven to be a very versatile system showing promising results in a growing number of cases. Indeed, its particular methylotrophic characteristics combined to the very simple handling of a eukaryotic microorganism that possesses the majority of mammalian-like machineries make it a very competitive expression system for various complex proteins, in amounts compatible with functional and structural studies. This chapter describes a set of robust methodologies routinely used for the successful expression of a variety of EMPs, going from yeast transformation with the recombinant plasmid to the analysis of the quality and quantity of the proteins produced.

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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 %
China 1 5%
Unknown 20 95%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 4 19%
Student > Ph. D. Student 4 19%
Student > Master 2 10%
Professor > Associate Professor 2 10%
Researcher 2 10%
Other 2 10%
Unknown 5 24%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 7 33%
Agricultural and Biological Sciences 7 33%
Chemical Engineering 1 5%
Neuroscience 1 5%
Unknown 5 24%
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 04 August 2016.
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#20,944,189
of 23,577,761 outputs
Outputs from Methods in molecular biology
#10,195
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#333,837
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Outputs of similar age from Methods in molecular biology
#1,077
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