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Membrane Proteins

Overview of attention for book
Cover of 'Membrane Proteins'

Table of Contents

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    Book Overview
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    Chapter 1 Use of Thiol-Disulfide Exchange Method to Study Transmembrane Peptide Association in Membrane Environments
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    Chapter 2 Measurement of Transmembrane Peptide Interactions in Liposomes Using Förster Resonance Energy Transfer (FRET).
  4. Altmetric Badge
    Chapter 3 Measuring Transmembrane Helix Interaction Strengths in Lipid Bilayers Using Steric Trapping
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    Chapter 4 Genetic Systems for Monitoring Interactions of Transmembrane Domains in Bacterial Membranes
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    Chapter 5 Analyzing the Effects of Hydrophobic Mismatch on Transmembrane α-Helices Using Tryptophan Fluorescence Spectroscopy.
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    Chapter 6 Folding alpha-helical membrane proteins into liposomes in vitro and determination of secondary structure.
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    Chapter 7 Solvation Models and Computational Prediction of Orientations of Peptides and Proteins in Membranes
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    Chapter 8 Membrane protein structure determination: back to the membrane.
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    Chapter 9 On the Role of NMR Spectroscopy for Characterization of Antimicrobial Peptides
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    Chapter 10 Prediction and Design of Outer Membrane Protein–Protein Interactions
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    Chapter 11 Design of Transmembrane Peptides: Coping with Sticky Situations
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    Chapter 12 Membrane Proteins
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    Chapter 13 Fluorination in the Design of Membrane Protein Assemblies
Attention for Chapter 6: Folding alpha-helical membrane proteins into liposomes in vitro and determination of secondary structure.
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Chapter title
Folding alpha-helical membrane proteins into liposomes in vitro and determination of secondary structure.
Chapter number 6
Book title
Membrane Proteins
Published in
Methods in molecular biology, August 2013
DOI 10.1007/978-1-62703-583-5_6
Pubmed ID
23975774
Book ISBNs
978-1-62703-582-8, 978-1-62703-583-5
Authors

Findlay HE, Booth PJ, Heather E. Findlay, Paula J. Booth

Abstract

The native environment of integral membrane proteins is a highly complex lipid bilayer composed of many different types of lipids, the physical characteristics of which can profoundly influence protein stability, folding, and function. Secondary transporters are a class of protein where changes to both structure and activity have been observed in different bilayer environments. In order to study these interactions in vitro, it is necessary to extract and purify the protein and exchange it into an artificial lipid system that can be manipulated to control protein behavior. Liposomes are a commonly used model system that is particularly suitable for studying transporters. GalP and LacY can be reconstituted or refolded into vesicles with a high degree of efficiency for further structural analysis. Circular dichroism spectroscopy is an important technique in monitoring protein folding, which allows the decomposition of spectra into secondary structural components.

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X Demographics

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 14 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 14 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 5 36%
Researcher 3 21%
Student > Bachelor 1 7%
Student > Master 1 7%
Unknown 4 29%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 29%
Agricultural and Biological Sciences 3 21%
Chemistry 2 14%
Unknown 5 36%
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 13 September 2013.
All research outputs
#18,347,414
of 22,721,584 outputs
Outputs from Methods in molecular biology
#7,857
of 13,083 outputs
Outputs of similar age
#149,473
of 200,084 outputs
Outputs of similar age from Methods in molecular biology
#31
of 59 outputs
Altmetric has tracked 22,721,584 research outputs across all sources so far. This one is in the 11th percentile – i.e., 11% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,083 research outputs from this source. They receive a mean Attention Score of 3.3. This one is in the 24th percentile – i.e., 24% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 200,084 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 12th percentile – i.e., 12% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 59 others from the same source and published within six weeks on either side of this one. This one is in the 23rd percentile – i.e., 23% of its contemporaries scored the same or lower than it.

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