Related ArticlesNMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol.
Biochemistry. 2004 Dec 7;43(48):15187-94
Authors: Booth V, Waring AJ, Walther FJ, Keough KM
Although the membrane-associated surfactant protein B (SP-B) is an essential component of lung surfactant, which is itself essential for life, the molecular basis for its activity is not understood. SP-B's biophysical functions can be partially mimicked by subfragments of the protein, including the C-terminus. We have used NMR to determine the structure of a C-terminal fragment of human SP-B that includes residues 63-78. Structure determination was performed both in the fluorinated alcohol hexafluoro-2-propanol (HFIP) and in sodium dodecyl sulfate (SDS) micelles. In both solvents, residues 68-78 take on an amphipathic helical structure, in agreement with predictions made by comparison to homologous saposin family proteins. In HFIP, the five N-terminal residues of the peptide are largely unstructured, while in SDS micelles, these residues take on a well-defined compact conformation. Differences in helical residue side chain positioning between the two solvents were also found, with better agreement between the structures for the hydrophobic face than the hydrophilic face. A paramagnetic probe was used to investigate the position of the peptide within the SDS micelles and indicated that the peptide is located at the water interface with the hydrophobic face of the helix oriented inward, the hydrophilic face of the helix oriented outward, and the N-terminal residues even farther from the micelle center than those on the hydrophilic face of the alpha-helix. Interactions of basic residues of SP-B with anionic lipid headgroups are known to have an impact on function, and these studies demonstrate structural ramifications of such interactions via the differences observed between the peptide structures determined in HFIP and SDS.
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
J Mol Biol. 2011 Apr 8;
Authors: Kryndushkin DS, Wickner RB, Tycko R
Intracellular fibril formation by Ure2p produces the non-Mendelian genetic element in Saccharomyces cerevisiae, making Ure2p a prion protein. We show that solid-state NMR spectra of full-length Ure2p fibrils, seeded...
nmrlearner
Journal club
0
04-19-2011 11:01 PM
[NMR paper] Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
Related Articles Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
Proteins. 2005 Jul 1;60(1):139-47
Authors: Garbuzynskiy SO, Melnik BS, Lobanov MY, Finkelstein AV, Galzitskaya OV
We have compared structures of 78 proteins determined by both NMR and X-ray methods. It is shown that X-ray and NMR structures...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] NMR study of a membrane protein in detergent-free aqueous solution.
NMR study of a membrane protein in detergent-free aqueous solution.
Related Articles NMR study of a membrane protein in detergent-free aqueous solution.
Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8893-8
Authors: Zoonens M, Catoire LJ, Giusti F, Popot JL
One of the major obstacles to membrane protein (MP) structural studies is the destabilizing effect of detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep MPs water-soluble under mild conditions. In the present work, we have explored the...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelle
Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
Related Articles Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
J Biomol NMR. 2002 Aug;23(4):289-301
Authors: Hilty C, Fernández C, Wider G, Wüthrich K
Sequence-specific assignments have been obtained for side chain methyl resonances of Val, Leu and Ile in the outer membrane protein X (OmpX) from Escherichia coli reconstituted in 60 kDa micelles in aqueous solution. Using previously established techniques, OmpX was...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[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...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] NMR observation of selected segments in a larger protein: central-segment isotope lab
NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation.
Related Articles NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation.
Biochemistry. 1999 Dec 7;38(49):16040-4
Authors: Otomo T, Ito N, Kyogoku Y, Yamazaki T
Peptide segments in a protein, which can include an active site of interest or be a series of parts constituting the entire structure, are now selectively observed by nuclear magnetic resonance...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[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...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] Light-induced membrane protein phosphorylation in the bovine rod outer segment. A mag
Light-induced membrane protein phosphorylation in the bovine rod outer segment. A magic angle spinning 31P-NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Light-induced membrane protein phosphorylation in the bovine rod outer segment. A magic angle spinning 31P-NMR study.
Biophys Chem. 1990 May;36(1):27-31
Authors: Albert AD, Frye JS, Yeagle PL
Magic angle spinning 31P-NMR (MAS 31P-NMR) spectra of bovine rod outer segments, unphosphorylated and...