From Proteopedia
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| | {{STRUCTURE_1dfw| PDB=1dfw | SCENE= }} | | {{STRUCTURE_1dfw| PDB=1dfw | SCENE= }} |
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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)'''
| + | ===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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10798379}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10798379 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10798379}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lung surfactant protein]] | | [[Category: Lung surfactant protein]] |
| | [[Category: Saposin]] | | [[Category: Saposin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:48:33 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:01:05 2008'' |
Revision as of 20:01, 30 June 2008
Template:STRUCTURE 1dfw
CONFORMATIONAL MAPPING OF THE N-TERMINAL SEGMENT OF SURFACTANT PROTEIN B IN LIPID USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)
Template:ABSTRACT PUBMED 10798379
About this Structure
1DFW is a Single protein structure. Full crystallographic information is available from OCA.
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:10798379
Page seeded by OCA on Mon Jun 30 23:01:05 2008
