External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface - Wikidata - awgldk - TriplyDB

External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface

External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface

http://www.wikidata.org/entity/Q34047825

about

Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy Effect of hydrophobic surfactant proteins SP-B and SP-C on phospholipid monolayers. Protein structure studied using 2D IR and beta correlation analysis.Critical structural and functional roles for the N-terminal insertion sequence in surfactant protein B analogs.Effect of hydrophobic surfactant peptides SP-B and SP-C on binary phospholipid monolayers. I. Fluorescence and dark-field microscopy.Effect of hydrophobic surfactant proteins SP-B and SP-C on binary phospholipid monolayers: II. Infrared external reflectance-absorption spectroscopy.Location of structural transitions in an isotopically labeled lung surfactant SP-B peptide by IRRAS.Deacylated pulmonary surfactant protein SP-C transforms from alpha-helical to amyloid fibril structure via a pH-dependent mechanism: an infrared structural investigation.Conformational changes in SP-B as a function of surface pressure.Fluorescently labeled pulmonary surfactant protein C in spread phospholipid monolayers Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid films Formation of three-dimensional protein-lipid aggregates in monolayer films induced by surfactant protein B.Critical structure-function determinants within the N-terminal region of pulmonary surfactant protein SP-B Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS).Spontaneous formation of interfacial lipid-protein monolayers during adsorption from vesicles.Structure of SP-B/DPPC mixed films studied by neutron reflectometry.Effects of palmitoylation on dynamics and phospholipid-bilayer-perturbing properties of the N-terminal segment of pulmonary surfactant protein SP-C as shown by 2H-NMR Structure and orientation of lung surfactant SP-C and L-alpha-dipalmitoylphosphatidylcholine in aqueous monolayers.External reflection Fourier transform infrared spectroscopy of surfactants at the air-water interface: separation of bulk and adsorbed surfactant signals.

P2860

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P2860

External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface

http://www.wikidata.org/entity/Q34047825

description

1995 nî lūn-bûn

@nan

1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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name

External reflection absorption ...... ers at the air/water interface

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External reflection absorption ...... ers at the air/water interface

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External reflection absorption ...... ers at the air/water interface

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type

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External reflection absorption ...... ers at the air/water interface

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External reflection absorption ...... ers at the air/water interface

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External reflection absorption ...... ers at the air/water interface

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External reflection absorption ...... ers at the air/water interface

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External reflection absorption ...... ers at the air/water interface

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External reflection absorption ...... ers at the air/water interface

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P1433

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S0006-3495(95)80124-4

P1433

Biophysical Journal

P1476

External reflection absorption ...... ers at the air/water interface

@en

P2093

A J Mautone

http://www.w3.org/2001/XMLSchema#string

B Pastrana-Rios

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K M Keough

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R Mendelsohn

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S Taneva

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix

Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attenuated total reflection infrared study.

External reflection FTIR of peptide monolayer films in situ at the air/water interface: experimental design, spectra-structure correlations, and effects of hydrogen-deuterium exchange.

Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption.

Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers.

Direct determination of surface tension in the lung.

Pulmonary surfactant-associated protein SP-B has little effect on acyl chains in dipalmitoylphosphatidylcholine dispersions.

Nonselective squeeze-out of dioleoylphosphatidylcholine and dioleoylphosphatidylglycerol from binary mixed monolayers with dipalmitoylphosphatidylcholine.

Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: I. Monolayers of pulmonary surfactant protein SP-B and phospholipids.

P304

2531-2540

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scholarly article

P356

10.1016/S0006-3495(95)80124-4

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P433

6

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P478

69

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1995-12-01T00:00:00Z

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P698

8599660

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P921

infrared spectroscopy

P932

1236491

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