Interactions of Hydrophobic Lung Surfactant Proteins SP-B and SP-C with Dipalmitoylphosphatidylcholine and Dipalmitoylphosphatidylglycerol Bilayers Studied by Electron Spin Resonance Spectroscopy-Reference-Cited by-同舟云学术

Interactions of Hydrophobic Lung Surfactant Proteins SP-B and SP-C with Dipalmitoylphosphatidylcholine and Dipalmitoylphosphatidylglycerol Bilayers Studied by Electron Spin Resonance Spectroscopy

Published:1995-03-28 Issue:12 Volume:34 Page:3964-3971
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Perez-Gil Jesus,Casals Cristina,Marsh Derek

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00012a014

Reference44 articles.

1. Surfactant protein SP-B induces ordering at the surface of model membrane bilayers

2. A high-sensitivity differential scanning calorimetric study of the interaction of melittin with dipalmitoylphosphatidylcholine fused unilamellar vesicles

3. Pulmonary Surfactant Protein B (SP-B): Structure-Function Relationships

4. Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant. Characterization and biophysical activity

5. Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups.

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