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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
  3. Altmetric Badge
    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
  5. Altmetric Badge
    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.
  7. Altmetric Badge
    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
  12. Altmetric Badge
    Chapter 11 Design of Transmembrane Peptides: Coping with Sticky Situations
  13. Altmetric Badge
    Chapter 12 Membrane Proteins
  14. Altmetric Badge
    Chapter 13 Fluorination in the Design of Membrane Protein Assemblies
Attention for Chapter 5: Analyzing the Effects of Hydrophobic Mismatch on Transmembrane α-Helices Using Tryptophan Fluorescence Spectroscopy.
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Chapter title
Analyzing the Effects of Hydrophobic Mismatch on Transmembrane α-Helices Using Tryptophan Fluorescence Spectroscopy.
Chapter number 5
Book title
Membrane Proteins
Published in
Methods in molecular biology, August 2013
DOI 10.1007/978-1-62703-583-5_5
Pubmed ID
23975773
Book ISBNs
978-1-62703-582-8, 978-1-62703-583-5
Authors

Caputo GA, Gregory A. Caputo

Abstract

Hydrophobic matching between transmembrane protein segments and the lipid bilayer in which they are embedded is a significant factor in the behavior and orientation of such transmembrane segments. The condition of hydrophobic mismatch occurs when the hydrophobic thickness of a lipid bilayer is significantly different than the length of the membrane spanning segment of a protein, resulting in a mismatch. This mismatch can result in altered function of proteins as well as nonnative structural arrangements including effects on transmembrane α-helix tilt angles, oligomerization state, and/or the formation of non-transmembrane topographies. Here, a fluorescence-based protocol is described for testing model transmembrane α-helices and their sensitivity to hydrophobic mismatch by measuring the propensity of these helices to form non-transmembrane structures. Overall, good hydrophobic matching between the bilayer and transmembrane segments is an important factor that must be considered when designing membrane proteins or peptides.

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X Demographics

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 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 5 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 5 100%

Demographic breakdown

Readers by professional status Count As %
Professor 1 20%
Student > Ph. D. Student 1 20%
Researcher 1 20%
Student > Doctoral Student 1 20%
Unknown 1 20%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 40%
Chemistry 1 20%
Unknown 2 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 02 March 2014.
All research outputs
#20,226,756
of 22,751,628 outputs
Outputs from Methods in molecular biology
#9,859
of 13,088 outputs
Outputs of similar age
#175,533
of 200,130 outputs
Outputs of similar age from Methods in molecular biology
#46
of 59 outputs
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So far Altmetric has tracked 13,088 research outputs from this source. They receive a mean Attention Score of 3.3. This one is in the 1st percentile – i.e., 1% of its peers scored the same or lower than it.
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