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

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

Item
http://www.wikidata.org/entity/Q34128648
Distinct behaviour of the homeodomain derived cell penetrating peptide penetratin in interaction with different phospholipidsThe infrared dichroism of transmembrane helical polypeptides.Calorimetric and spectroscopic studies of the thermotropic phase behavior of lipid bilayer model membranes composed of a homologous series of linear saturated phosphatidylserines.Differential scanning calorimetric and Fourier transform infrared spectroscopic studies of the effects of cholesterol on the thermotropic phase behavior and organization of a homologous series of linear saturated phosphatidylserine bilayer membranesEffect of variations in the structure of a polyleucine-based alpha-helical transmembrane peptide on its interaction with phosphatidylethanolamine Bilayers.Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring.Studies of the minimum hydrophobicity of alpha-helical peptides required to maintain a stable transmembrane association with phospholipid bilayer membranes.SARS-CoV fusion peptides induce membrane surface ordering and curvature.Orientation and dynamics of transmembrane peptides: the power of simple models.Structural and functional characterization of transmembrane segment VII of the Na+/H+ exchanger isoform 1.Cluster analysis identifies aminoacid compositional features that indicate Toxoplasma gondii adhesin proteins.The effects of ethylene oxide containing lipopolymers and tri-block copolymers on lipid bilayers of dipalmitoylphosphatidylcholine.Polar residue tagging of transmembrane peptides.Translocation of amino acyl residues from the membrane interface to the hydrophobic core: thermodynamic model and experimental analysis using ATR-FTIR spectroscopy.
P2860

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

Item
http://www.wikidata.org/entity/Q34128648
description
1995 nî lūn-bûn
@nan
1995 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մարտին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Interaction of a peptide model ...... infrared spectroscopic studies
@ast
Interaction of a peptide model ...... infrared spectroscopic studies
@en
Interaction of a peptide model ...... infrared spectroscopic studies
@nl
type
label
Interaction of a peptide model ...... infrared spectroscopic studies
@ast
Interaction of a peptide model ...... infrared spectroscopic studies
@en
Interaction of a peptide model ...... infrared spectroscopic studies
@nl
prefLabel
Interaction of a peptide model ...... infrared spectroscopic studies
@ast
Interaction of a peptide model ...... infrared spectroscopic studies
@en
Interaction of a peptide model ...... infrared spectroscopic studies
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P1476
P2093
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Interaction of a peptide model ...... infrared spectroscopic studies
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P2093
P2860
P304
P31
P356
10.1016/S0006-3495(95)80261-4
P407
P433
P478
P577
P698
P921
P932