pubmed-article:12829488 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C0034085 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C0450429 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C1442757 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C1708632 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
pubmed-article:12829488 | lifeskim:mentions | umls-concept:C1522485 | lld:lifeskim |
pubmed-article:12829488 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:12829488 | pubmed:dateCreated | 2003-6-27 | lld:pubmed |
pubmed-article:12829488 | pubmed:abstractText | Pulmonary surfactant, a lipid/protein complex that lines the air/water interface in the mammalian lung, functions to reduce the work of breathing. Surfactant protein B (SP-B) is a small, hydrophobic protein that is an essential component of this mixture. Structure-function relationships of SP-B are currently under investigation as the protein and its peptide analogs are being incorporated into surfactant replacement therapies. Knowledge of the structure of SP-B and its related peptides in bulk and monolayer phases will facilitate the design of later generation therapeutic agents. Prior infrared reflection-absorption spectroscopic studies reported notable, reversible surface pressure-induced antiparallel beta-sheet formation in a synthetic peptide derived from human SP-B, residues 9-36 (SP-B(9-36)). In the current work, infrared reflection-absorption spectroscopy is applied in conjunction with isotopic labeling to detect the site and pressure dependence of the conformational change. SP-B(9-36), synthesized with (13)C=O-labeled Ala residues in positions 26, 28, 30, and 32, shifted the beta-sheet marker band to approximately 1600 cm(-1) and thus immediately identified this structural element within the labeled region. Surface pressure-induced alterations in the relative intensities of Amide I band constituents are interpreted using a semiempirical transition dipole coupling model. In addition, electron micrographs reveal the formation of tubular myelin structures from in vitro preparations using SP-B(9-36) in place of porcine SP-B indicating that the peptide has the potential to mimic this property of the native protein. | lld:pubmed |
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pubmed-article:12829488 | pubmed:language | eng | lld:pubmed |
pubmed-article:12829488 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12829488 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12829488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12829488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12829488 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12829488 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12829488 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12829488 | pubmed:issn | 0006-3495 | lld:pubmed |
pubmed-article:12829488 | pubmed:author | pubmed-author:FlachCarol... | lld:pubmed |
pubmed-article:12829488 | pubmed:author | pubmed-author:MendelsohnRic... | lld:pubmed |
pubmed-article:12829488 | pubmed:author | pubmed-author:CaiPengP | lld:pubmed |
pubmed-article:12829488 | pubmed:author | pubmed-author:DieudonnéDarl... | lld:pubmed |
pubmed-article:12829488 | pubmed:author | pubmed-author:BraunerJoseph... | lld:pubmed |
pubmed-article:12829488 | pubmed:author | pubmed-author:KeoughKevin... | lld:pubmed |
pubmed-article:12829488 | pubmed:author | pubmed-author:StewartJuneJ | lld:pubmed |
pubmed-article:12829488 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12829488 | pubmed:volume | 85 | lld:pubmed |
pubmed-article:12829488 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12829488 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12829488 | pubmed:pagination | 340-9 | lld:pubmed |
pubmed-article:12829488 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:12829488 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12829488 | pubmed:articleTitle | Location of structural transitions in an isotopically labeled lung surfactant SP-B peptide by IRRAS. | lld:pubmed |
pubmed-article:12829488 | pubmed:affiliation | Department of Chemistry, Newark College of Arts and Sciences, Rutgers University, Newark, New Jersey, USA. flach@andromeda.rutgers.edu | lld:pubmed |
pubmed-article:12829488 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12829488 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:12829488 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12829488 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:12829488 | pubmed:publicationType | Evaluation Studies | lld:pubmed |