(Q34187329)

English

Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine Bilayers

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scholarly article

1 reference

Europe PubMed Central

31 July 2017

Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine Bilayers (English)

1 reference

Europe PubMed Central

31 July 2017

transmembrane protein

0 references

author name string

Feng Liu

1

1 reference

Europe PubMed Central

31 July 2017

Ruthven N A H Lewis

2

1 reference

Europe PubMed Central

31 July 2017

Robert S Hodges

3

1 reference

Europe PubMed Central

31 July 2017

Ronald N McElhaney

4

1 reference

Europe PubMed Central

31 July 2017

language of work or name

0 references

publication date

1 October 2004

1 reference

Europe PubMed Central

31 July 2017

number of pages

13

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based on heuristic

inferred from page(s)

Biophysical Journal

1 reference

Europe PubMed Central

31 July 2017

87

1 reference

Europe PubMed Central

31 July 2017

4

1 reference

Europe PubMed Central

31 July 2017

2470-2482

1 reference

Europe PubMed Central

31 July 2017

Protein–lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring (Review)

1 reference

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Protein-lipid interactions in the purple bacterial reaction centre

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Peptide models of the helical hydrophobic transmembrane segments of membrane proteins: interactions of acetyl-K2-(LA)12-K2-amide with phosphatidylethanolamine bilayer membranes

1 reference

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How proteins adapt to a membrane-water interface

1 reference

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Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease

1 reference

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Infrared spectroscopy of proteins and peptides in lipid bilayers

1 reference

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The infrared dichroism of transmembrane helical polypeptides

1 reference

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Calorimetric and spectroscopic studies of the polymorphic phase behavior of a homologous series of n-saturated 1,2-diacyl phosphatidylethanolamines

1 reference

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Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylethanolamine bilayers: differential scanning calorimetric and Fourier transform infrared spectroscopic studies

1 reference

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Simultaneous modeling of phase and calorimetric behavior in an amphiphilic peptide/phospholipid model membrane.

1 reference

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Effect of lipid structural modifications on their intermolecular hydrogen bonding interactions and membrane functions

1 reference

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Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function

1 reference

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Specificity of lipid-protein interactions as determined by spectroscopic techniques

1 reference

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Lipids of mitochondria

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Quenching of tryptophan fluorescence by brominated phospholipid

1 reference

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Amphipathic helix motif: classes and properties

1 reference

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Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylcholine bilayers: differential scanning calorimetric and FTIR spectroscopic studies

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1304667

5 July 2018

Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylglycerol bilayers

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1304667

28 October 2018

Reversible topological organization within a polytopic membrane protein is governed by a change in membrane phospholipid composition

1 reference

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Molecular dynamics of 1-palmitoyl-2-oleoylphosphatidylcholine membranes containing transmembrane alpha-helical peptides with alternating leucine and alanine residues

1 reference

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28 October 2018

Effect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1304667

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1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1304667

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/15454444

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1 reference

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Membrane proteins: from sequence to structure

1 reference

https://pubmed.ncbi.nlm.nih.gov/15454444

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Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers

1 reference

https://pubmed.ncbi.nlm.nih.gov/15454444

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Transmembrane orientation of hydrophobic alpha-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration

1 reference

https://pubmed.ncbi.nlm.nih.gov/15454444

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Molecular organization and dynamics of 1-palmitoyl-2-oleoylphosphatidylcholine bilayers containing a transmembrane alpha-helical peptide

1 reference

https://pubmed.ncbi.nlm.nih.gov/15454444

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Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling

1 reference

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inferred from PubMed ID database lookup

Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix

1 reference

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Intensities and other spectral parameters of infrared amide bands of polypeptides in the alpha-helical form

1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/15454444

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1 reference

https://pubmed.ncbi.nlm.nih.gov/15454444

12 December 2020

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Identifiers

10.1529/BIOPHYSJ.104.046342

1 reference

Europe PubMed Central

31 July 2017

1 reference

Europe PubMed Central

31 July 2017

1 reference

Europe PubMed Central

31 July 2017

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