Related ArticlesThe 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 32:64:5 (v/v). Sequence-specific 1H NMR assignments and the collection of conformational constraints were achieved with two-dimensional 1H NMR, and the structure was calculated with the distance geometry program DIANA. The root mean square deviations for the well-defined polypeptide segment of residues 9-34 calculated for the 20 best energy-minimized DIANA conformers relative to their mean are 0.5 and 1.3 A for the polypeptide backbone atoms N, C alpha, and C', and for all heavy atoms, respectively. The 35-residue polypeptide chain of SP-C forms an alpha-helix between positions 9 and 34, which includes two segments of seven and four consecutive valyls that are separated by a single leucyl residue. The N-terminal hexapeptide segment, which includes two palmitoylcysteinyls, is flexibly disordered. The length of the alpha-helix is about 37 A, and the helical segment of residues 13-28, which contains exclusively aliphatic residues with branched side chains, is 23-A long and about 10 A in diameter. The alpha-helix is outstandingly regular, with virtually identical chi 1 angles for all valyl residues. The observation of a helical structure of SP-C was rather unexpected, considering that Val is generally underrepresented in alpha-helices, and it provides intriguing novel insights into the structural basis of SP-C functions as well as into general structural aspects of protein-lipid interactions in biological membranes.
[NMR paper] Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysi
Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Related Articles Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Biopolymers. 2003 Oct;70(2):158-68
Authors: Hong M, Isailovic D, McMillan RA, Conticello VP
The conformation of an elastin-mimetic recombinant protein, 39, is investigated using solid-state NMR spectroscopy. The protein is extensively labeled with 13C and 15N, and two-dimensional 13C-13C and 15N-13C correlation experiments were carried out to resolve and...
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[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] High-resolution polypeptide structure in a lamellar phase lipid environment from soli
High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints.
Related Articles High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints.
Structure. 1997 Dec 15;5(12):1655-69
Authors: Ketchem R, Roux B, Cross T
BACKGROUND: Solid-state nuclear magnetic resonance (NMR) spectroscopy provides novel structural constraints from uniformly aligned samples. These orientational constraints orient specific atomic...
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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] NMR determination of the secondary structure and the three-dimensional polypeptide ba
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
FEBS Lett. 1993 Nov 29;335(1):18-26
Authors: Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wüthrich K
Nuclear magnetic resonance (NMR)...
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[NMR paper] 2H NMR studies of the effect of pulmonary surfactant SP-C on the 1,2-dipalmitoyl-sn-g
2H 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.
Related Articles 2H 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.
Biochemistry. 1993 Oct 26;32(42):11338-44
Authors: Morrow MR, Taneva S, Simatos GA, Allwood LA, Keough KM
Surfactant protein C (SP-C) was...
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[NMR paper] Polypeptide backbone resonance assignments and secondary structure of Bacillus subtil
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Related Articles Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1991 Jul 16;30(28):6896-907
Authors: Fairbrother WJ, Cavanagh J, Dyson HJ, Palmer AG, Sutrina SL, Reizer J, Saier MH, Wright PE
The enzyme...
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[NMR paper] Polypeptide backbone resonance assignments and secondary structure of Bacillus subtil
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Related Articles Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1991 Jul 16;30(28):6896-907
Authors: Fairbrother WJ, Cavanagh J, Dyson HJ, Palmer AG, Sutrina SL, Reizer J, Saier MH, Wright PE
The enzyme...