1dfw
From Proteopedia
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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)
Contents |
Overview
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
Known disease associated with this structure: Surfactant metabolism dysfunction, pulmonary, 1 OMIM:[178640]
About this Structure
1DFW is a Single protein structure of sequence from [1]. 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 Nov 12 16:31:59 2007
