Related Articles2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-glycero-3-phosphocholine headgroup: a model for transbilayer peptides in surfactant and biological membranes.
Surfactant protein C (SP-C) was isolated from solvent extracts of porcine pulmonary surfactant by gel filtration chromatography. The surfactant protein was combined with dipalmitoylphosphatidylcholine deuterated at the alpha and beta positions of the choline headgroup (DPPC-d4) Deuterium nuclear magnetic resonance spectra were collected as a function of temperature for a series of protein concentrations. The splitting of the alpha-deuteron spectrum in the liquid-crystalline phase was insensitive to temperature but decreased with increasing protein concentration. The response of headgroup conformation to protein concentration was consistent with an interaction between the lipid headgroup dipole and the net positive surface charge associated with the protein. The observed effect per charge on the alpha splitting was less than that reported for singly-charged amphiphiles [Scherer, P. G., & Seelig, J. (1989) Biochemistry 28, 7720-7728] but was similar to that obtained using a multipled-charged amphiphilic polypeptide [Roux, M., Neumann, J.-M., Hodges, R. S., Devaux, P. F., & Bloom, M. (1989) Biochemistry 28, 2313-2321]. This comparison suggests that the charges on SP-C are located near the bilayer surface. The possibility that the headgroup response is sensitive to the degree of clustering of surface charge is discussed. The beta-deuteron splitting in the liquid-crystalline phase decreased with increasing temperature but was relatively insensitive to protein concentration, suggesting that the torsion angle about the C alpha-C beta bond might be sensitive to steric interactions between the lipid headgroup and the protein.
[NMR paper] NMR structure of lung surfactant peptide SP-B(11-25).
NMR structure of lung surfactant peptide SP-B(11-25).
Related Articles NMR structure of lung surfactant peptide SP-B(11-25).
Biochemistry. 2002 Jul 30;41(30):9627-36
Authors: Kurutz JW, Lee KY
Surfactant protein B (SP-B) is a 79-residue essential component of lung surfactant, the film of lipid and protein lining the alveoli, and is the subject of great interest for its role in lung surfactant replacement therapies. Here we report circular dichroism results and the solution NMR structure of SP-B(11-25) (CRALIKRIQAMIPKG) dissolved in CD(3)OH at...
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[NMR paper] What NMR can tell us about where lung surfactant proteins live.
What NMR can tell us about where lung surfactant proteins live.
Related Articles What NMR can tell us about where lung surfactant proteins live.
Biochem Soc Trans. 1997 Aug;25(3):1103-7
Authors: Morrow MR, Taneva S, Dico AS, Hancock J, Keough KM
2H-NMR is beginning to provide some insights into the way in which the hydrophobic surfactant proteins SP-B and SP-C interact with phospholipid bilayers in multilamellar structures. Both proteins have a significant effect on slow bilayer motions. In many ways, the effect of SP-C on the surrounding...
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[NMR paper] The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apola
The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.
Related Articles The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.
Biochemistry. 1994 May 17;33(19):6015-23
Authors: Johansson J, Szyperski T, Curstedt T, Wüthrich K
The nuclear magnetic resonance (NMR) structure of the pulmonary surfactant-associated lipoplypeptide C (SP-C) was determined in a mixed solvent of C2H3Cl/C2H3OH/ 1 M HCl...
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[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
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[NMR paper] The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apola
The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.
Related Articles The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.
Biochemistry. 1994 May 17;33(19):6015-23
Authors: Johansson J, Szyperski T, Curstedt T, Wüthrich K
The nuclear magnetic resonance (NMR) structure of the pulmonary surfactant-associated lipoplypeptide C (SP-C) was determined in a mixed solvent of C2H3Cl/C2H3OH/ 1 M HCl...
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08-22-2010 03:33 AM
[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
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[NMR paper] Proton NMR studies of the structural and dynamical effect of chemical modification of
Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin. Relation to the structure of the putative binding site and the cytolytic activity of the toxin.
Related Articles Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin. Relation to the structure of the putative binding site and the cytolytic activity of the toxin.
J Mol Biol. 1994 Nov 4;243(4):719-35
Authors: Roumestand C, Gilquin B,...
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[NMR paper] 1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of
1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of Au(I) and Cu(I) diphosphine complexes on the cell metabolism.
Related Articles 1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of Au(I) and Cu(I) diphosphine complexes on the cell metabolism.
Magn Reson Med. 1991 Mar;18(1):142-58
Authors: Berners-Price SJ, Sant ME, Christopherson RI, Kuchel PW
The effect of the antitumor complex Cl (where dppe is Ph2P(CH2)2PPh2) on the overall metabolism of cultured mouse L1210 leukemia cells...
2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-g
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