1dfw: Difference between revisions
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New page: left|200px<br /> <applet load="1dfw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfw" /> '''CONFORMATIONAL MAPPING OF THE N-TERMINAL SE... |
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[[Image:1dfw.gif|left|200px]]<br /> | [[Image:1dfw.gif|left|200px]]<br /><applet load="1dfw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)'''<br /> | '''CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)'''<br /> | ||
==Overview== | ==Overview== | ||
Synthetic peptides based on the N-terminal domain of human surfactant | Synthetic peptides based on the N-terminal domain of human surfactant protein B (SP-B1-25; 25 amino acid residues; NH2-FPIPLPYCWLCRALIKRIQAMIPKG) retain important lung activities of the full-length, 79-residue protein. Here, we used physical techniques to examine the secondary conformation of SP-B1-25 in aqueous, lipid and structure-promoting environments. Circular dichroism and conventional, 12C-Fourier transform infrared (FTIR) spectroscopy each indicated a predominate alpha-helical conformation for SP-B1-25 in phosphate-buffered saline, liposomes of 1-palmitoyl-2-oleoyl phosphatidylglycerol and the structure-promoting solvent hexafluoroisopropanol; FTIR spectra also showed significant beta- and random conformations for peptide in these three environments. In further experiments designed to map secondary structure to specific residues, isotope-enhanced FTIR spectroscopy was performed with 1-palmitoyl-2-oleoyl phosphatidylglycerol liposomes and a suite of SP-B1-25 peptides labeled with 13C-carbonyl groups at either single or multiple sites. Combining these 13C-enhanced FTIR results with energy minimizations and molecular simulations indicated the following model for SP-B1-25 in 1-palmitoyl-2-oleoyl phosphatidylglycerol: beta-sheet (residues 1-6), alpha-helix (residues 8-22) and random (residues 23-25) conformations. Analogous structural motifs are observed in the corresponding homologous N-terminal regions of several proteins that also share the 'saposin-like' (i.e. 5-helix bundle) folding pattern of full-length, human SP-B. In future studies, 13C-enhanced FTIR spectroscopy and energy minimizations may be of general use in defining backbone conformations at amino acid resolution, particularly for peptides or proteins in membrane environments. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1DFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1DFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFW OCA]. | ||
==Reference== | ==Reference== | ||
Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy., Gordon LM, Lee KY, Lipp MM, Zasadzinski JA, Walther FJ, Sherman MA, Waring AJ, J Pept Res. 2000 Apr;55(4):330-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10798379 10798379] | Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy., Gordon LM, Lee KY, Lipp MM, Zasadzinski JA, Walther FJ, Sherman MA, Waring AJ, J Pept Res. 2000 Apr;55(4):330-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10798379 10798379] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gordon, L | [[Category: Gordon, L M.]] | ||
[[Category: Lee, K | [[Category: Lee, K Y.C.]] | ||
[[Category: Lipp, M | [[Category: Lipp, M M.]] | ||
[[Category: Sherman, M | [[Category: Sherman, M A.]] | ||
[[Category: Walther, F | [[Category: Walther, F J.]] | ||
[[Category: Waring, A | [[Category: Waring, A J.]] | ||
[[Category: Zasadzinski, J | [[Category: Zasadzinski, J A.]] | ||
[[Category: lung surfactant protein]] | [[Category: lung surfactant protein]] | ||
[[Category: saposin]] | [[Category: saposin]] | ||
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