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Heterologous Gene Expression in E.coli

Overview of attention for book
Cover of 'Heterologous Gene Expression in E.coli'

Table of Contents

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    Book Overview
  2. Altmetric Badge
    Chapter 1 Recombinant Protein Expression in E. coli : A Historical Perspective
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    Chapter 2 N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools
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    Chapter 3 Harnessing the Profinity eXact™ System for Expression and Purification of Heterologous Proteins in E. coli
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    Chapter 4 ESPRIT: A Method for Defining Soluble Expression Constructs in Poorly Understood Gene Sequences
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    Chapter 5 Optimizing Expression and Solubility of Proteins in E. coli Using Modified Media and Induction Parameters
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    Chapter 6 Optimization of Membrane Protein Production Using Titratable Strains of E. coli
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    Chapter 7 Optimizing E. coli-Based Membrane Protein Production Using Lemo21(DE3) or pReX and GFP-Fusions
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    Chapter 8 High Yield of Recombinant Protein in Shaken E. coli Cultures with Enzymatic Glucose Release Medium EnPresso B
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    Chapter 9 A Generic Protocol for Purifying Disulfide-Bonded Domains and Random Protein Fragments Using Fusion Proteins with SUMO3 and Cleavage by SenP2 Protease
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    Chapter 10 A Strategy for Production of Correctly Folded Disulfide-Rich Peptides in the Periplasm of E. coli
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    Chapter 11 Split GFP Complementation as Reporter of Membrane Protein Expression and Stability in E. coli: A Tool to Engineer Stability in a LAT Transporter
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    Chapter 12 Acting on Folding Effectors to Improve Recombinant Protein Yields and Functional Quality
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    Chapter 13 Protein Folding Using a Vortex Fluidic Device
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    Chapter 14 Removal of Affinity Tags with TEV Protease
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    Chapter 15 Generation of Recombinant N-Linked Glycoproteins in E. coli
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    Chapter 16 Production of Protein Kinases in E. coli
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    Chapter 17 Expression of Prokaryotic Integral Membrane Proteins in E. coli
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    Chapter 18 Multiprotein Complex Production in E. coli: The SecYEG-SecDFYajC-YidC Holotranslocon
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    Chapter 19 Membrane Protein Production in E. coli Lysates in Presence of Preassembled Nanodiscs
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    Chapter 20 Not Limited to E. coli: Versatile Expression Vectors for Mammalian Protein Expression
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    Chapter 21 A Generic Protocol for Intracellular Expression of Recombinant Proteins in Bacillus subtilis
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    Chapter 22 In Vivo Biotinylation of Antigens in E. coli
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    Chapter 23 Cold-Shock Expression System in E. coli for Protein NMR Studies
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    Chapter 24 High-Throughput Production of Proteins in E. coli for Structural Studies
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    Chapter 25 Mass Spectrometric Analysis of Proteins
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    Chapter 26 How to Determine Interdependencies of Glucose and Lactose Uptake Rates for Heterologous Protein Production with E. coli
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    Chapter 27 Interfacing Biocompatible Reactions with Engineered Escherichia coli
Attention for Chapter 2: N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools
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Chapter title
N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools
Chapter number 2
Book title
Heterologous Gene Expression in E.coli
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-6887-9_2
Pubmed ID
28470596
Book ISBNs
978-1-4939-6885-5, 978-1-4939-6887-9, 978-1-4939-6885-5, 978-1-4939-6887-9
Authors

Christopher D. O. Cooper, Brian D. Marsden

Editors

Nicola A. Burgess-Brown

Abstract

Soluble protein expression is a key requirement for biochemical and structural biology approaches to study biological systems in vitro. Production of sufficient quantities may not always be achievable if proteins are poorly soluble which is frequently determined by physico-chemical parameters such as intrinsic disorder. It is well known that discrete protein domains often have a greater likelihood of high-level soluble expression and crystallizability. Determination of such protein domain boundaries can be challenging for novel proteins. Here, we outline the application of bioinformatics tools to facilitate the prediction of potential protein domain boundaries, which can then be used in designing expression construct boundaries for parallelized screening in a range of heterologous expression systems.

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X Demographics

The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 25 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 25 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 6 24%
Student > Ph. D. Student 3 12%
Lecturer > Senior Lecturer 2 8%
Student > Postgraduate 2 8%
Student > Master 1 4%
Other 1 4%
Unknown 10 40%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 9 36%
Agricultural and Biological Sciences 5 20%
Business, Management and Accounting 1 4%
Unknown 10 40%
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 22 February 2018.
All research outputs
#15,457,417
of 22,968,808 outputs
Outputs from Methods in molecular biology
#5,377
of 13,142 outputs
Outputs of similar age
#257,202
of 421,088 outputs
Outputs of similar age from Methods in molecular biology
#468
of 1,074 outputs
Altmetric has tracked 22,968,808 research outputs across all sources so far. This one is in the 22nd percentile – i.e., 22% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,142 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 44th percentile – i.e., 44% of its peers scored the same or lower than it.
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We're also able to compare this research output to 1,074 others from the same source and published within six weeks on either side of this one. This one is in the 40th percentile – i.e., 40% of its contemporaries scored the same or lower than it.

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