The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix
about
High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.The surfactant peptide KL4 in lipid monolayers: phase behavior, topography, and chemical distributionSuperficial disposition of the N-terminal region of the surfactant protein SP-C and the absence of specific SP-B-SP-C interactions in phospholipid bilayersBiosynthesis of surfactant protein C (SP-C). Sorting of SP-C proprotein involves homomeric association via a signal anchor domainEffect of hydrophobic surfactant proteins SP-B and SP-C on phospholipid monolayers. Protein structure studied using 2D IR and beta correlation analysis.Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.Specific chaperones and regulatory domains in control of amyloid formation.A solvent model for simulations of peptides in bilayers. II. Membrane-spanning alpha-helices.Efficient protein production inspired by how spiders make silkHydrogen/deuterium exchange and aggregation of a polyvaline and a polyleucine alpha-helix investigated by matrix-assisted laser desorption ionization mass spectrometry.Biophysical activity of an artificial surfactant containing an analogue of surfactant protein (SP)-C and native SP-BExternal reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interfaceDimeric N-terminal segment of human surfactant protein B (dSP-B(1-25)) has enhanced surface properties compared to monomeric SP-B(1-25)Effect of hydrophobic surfactant proteins SP-B and SP-C on binary phospholipid monolayers: II. Infrared external reflectance-absorption spectroscopy.Deacylated pulmonary surfactant protein SP-C transforms from alpha-helical to amyloid fibril structure via a pH-dependent mechanism: an infrared structural investigation.Biophysical mimicry of lung surfactant protein B by random nylon-3 copolymersMolecular dynamics of surfactant protein C: from single molecule to heptameric aggregates.Biomimetic N-terminal alkylation of peptoid analogues of surfactant protein CAn elevated level of cholesterol impairs self-assembly of pulmonary surfactant into a functional film.NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain.Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopyFluorescently labeled pulmonary surfactant protein C in spread phospholipid monolayersHydrophobic surfactant proteins and their analogues.Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid filmsTransthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.Analysis of lung surfactant model systems with time-of-flight secondary ion mass spectrometry.Fluorescence light microscopy of pulmonary surfactant at the air-water interface of an air bubble of adjustable size.Effects of oligomerization and secondary structure on the surface behavior of pulmonary surfactant proteins SP-B and SP-C.Expression of a human surfactant protein C mutation associated with interstitial lung disease disrupts lung development in transgenic mice.Biomimicry of surfactant protein C.Synthetic protein analogues in artificial surfactants.Chemical shift assignment and structural plasticity of a HIV fusion peptide derivative in dodecylphosphocholine micellesThe N-terminal segment of pulmonary surfactant lipopeptide SP-C has intrinsic propensity to interact with and perturb phospholipid bilayers.Direct simulation of protein-mediated vesicle fusion: lung surfactant protein BSecondary structure and biophysical activity of synthetic analogues of the pulmonary surfactant polypeptide SP-CEffect of Lung Surfactant Protein SP-C and SP-C-Promoted Membrane Fragmentation on Cholesterol Dynamics.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-NMRThe surfactant peptide KL4 sequence is inserted with a transmembrane orientation into the endoplasmic reticulum membraneSurfactant protein C peptides with salt-bridges ("ion-locks") promote high surfactant activities by mimicking the α-helix and membrane topography of the native proteinPulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric alpha-helical state into insoluble beta-sheet aggregates.
P2860
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P2860
The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@ast
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@en
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@nl
type
label
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@ast
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@en
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@nl
prefLabel
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@ast
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@en
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@nl
P50
P3181
P356
P1433
P1476
The NMR structure of the pulmo ...... tains a valyl-rich alpha-helix
@en
P2093
T Curstedt
P304
P3181
P356
10.1021/BI00185A042
P407
P577
1994-05-17T00:00:00Z