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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 />
<applet load="1dfw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dfw" />
'''CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)'''<br />


==Overview==
==CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)==
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.
<StructureSection load='1dfw' size='340' side='right'caption='[[1dfw]]' scene=''>
 
== Structural highlights ==
==Disease==
<table><tr><td colspan='2'>[[1dfw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DFW FirstGlance]. <br>
Known disease associated with this structure: Surfactant metabolism dysfunction, pulmonary, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=178640 178640]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Infrared spectroscopy</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfw OCA], [https://pdbe.org/1dfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dfw RCSB], [https://www.ebi.ac.uk/pdbsum/1dfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dfw ProSAT]</span></td></tr>
==About this Structure==
</table>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DFW OCA].
== Disease ==
 
[https://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN] Defects in SFTPB are the cause of pulmonary surfactant metabolism dysfunction type 1 (SMDP1) [MIM:[https://omim.org/entry/265120 265120]; also called pulmonary alveolar proteinosis due to surfactant protein B deficiency. A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress.<ref>PMID:7491219</ref>  Genetic variations in SFTPB are a cause of susceptibility to respiratory distress syndrome in premature infants (RDS) [MIM:[https://omim.org/entry/267450 267450]. RDS is a lung disease affecting usually premature newborn infants. It is characterized by deficient gas exchange, diffuse atelectasis, high-permeability lung edema and fibrin-rich alveolar deposits called 'hyaline membranes'. Note=A variation Ile to Thr at position 131 influences the association between specific alleles of SFTPA1 and respiratory distress syndrome in premature infants.<ref>PMID:11063734</ref>
==Reference==
== Function ==
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]
[https://www.uniprot.org/uniprot/PSPB_HUMAN PSPB_HUMAN] Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter.
[[Category: Single protein]]
== References ==
[[Category: Gordon, L.M.]]
<references/>
[[Category: Lee, K.Y.C.]]
__TOC__
[[Category: Lipp, M.M.]]
</StructureSection>
[[Category: Sherman, M.A.]]
[[Category: Homo sapiens]]
[[Category: Walther, F.J.]]
[[Category: Large Structures]]
[[Category: Waring, A.J.]]
[[Category: Gordon LM]]
[[Category: Zasadzinski, J.A.]]
[[Category: Lee KYC]]
[[Category: lung surfactant protein]]
[[Category: Lipp MM]]
[[Category: saposin]]
[[Category: Sherman MA]]
 
[[Category: Walther FJ]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:31:59 2007''
[[Category: Waring AJ]]
[[Category: Zasadzinski JA]]

Latest revision as of 06:53, 7 February 2024

CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)

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