| pubmed-article:7980429 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7980429 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:7980429 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:7980429 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:7980429 | lifeskim:mentions | umls-concept:C0024544 | lld:lifeskim |
| pubmed-article:7980429 | lifeskim:mentions | umls-concept:C1710466 | lld:lifeskim |
| pubmed-article:7980429 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:7980429 | pubmed:dateCreated | 1994-11-30 | lld:pubmed |
| pubmed-article:7980429 | pubmed:abstractText | A peptide corresponding to the N-terminal sequence of the rat malate dehydrogenase, comprising the transit sequence and two residues of the mature protein (MLSALARPVGAALR-RSFSTSAQNNAK) has been chemically synthesized, and its structural characteristics investigated by Fourier-transform i.r. (FT-IR), c.d. and 1H-n.m.r. spectroscopy. FT-IR and c.d. spectra of the peptide were recorded in a variety of environments (aqueous solution, trifluoroethanol) and after incorporation into phospholipid bilayers. The peptide was found to be mainly in aperiodic or undefined conformation in aqueous solution. However, in trifluoroethanol a marked increase in alpha-helical content was observed. An increase in alpha-helical content was also observed in negatively charged lipids (dimyristoylphosphatidylglycerol and cardiolipin). However, when reconstituted in a zwitterionic phospholipid (dimyristoylphosphatidylcholine), no alpha-helical structure was observed. N.m.r. spectroscopy was used to characterize the helical structure in greater detail in trifluoroethanol. The 1H-n.m.r. spectrum of the peptide in this solvent was assigned using standard homonuclear two-dimensional methods. The observed patterns of nuclear Overhauser enhancements confirmed the deductions obtained from c.d. and FT-1R spectroscopy concerning the solution conformation, suggesting a region of flexible nascent helix between Ala-4 and Ser-18. This structure is discussed in terms of the possible function of the peptide. | lld:pubmed |
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| pubmed-article:7980429 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7980429 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7980429 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7980429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7980429 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7980429 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7980429 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7980429 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7980429 | pubmed:author | pubmed-author:LucyJ AJA | lld:pubmed |
| pubmed-article:7980429 | pubmed:author | pubmed-author:AustenB MBM | lld:pubmed |
| pubmed-article:7980429 | pubmed:author | pubmed-author:ReidD GDG | lld:pubmed |
| pubmed-article:7980429 | pubmed:author | pubmed-author:WhiteJJ | lld:pubmed |
| pubmed-article:7980429 | pubmed:author | pubmed-author:ChapmanDD | lld:pubmed |
| pubmed-article:7980429 | pubmed:author | pubmed-author:MacLachlanL... | lld:pubmed |
| pubmed-article:7980429 | pubmed:author | pubmed-author:HarisP IPI | lld:pubmed |
| pubmed-article:7980429 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7980429 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7980429 | pubmed:volume | 303 ( Pt 2) | lld:pubmed |
| pubmed-article:7980429 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7980429 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7980429 | pubmed:pagination | 657-62 | lld:pubmed |
| pubmed-article:7980429 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7980429 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7980429 | pubmed:articleTitle | A spectroscopic study of the mitochondrial transit peptide of rat malate dehydrogenase. | lld:pubmed |
| pubmed-article:7980429 | pubmed:affiliation | SmithKline Beecham Pharmaceuticals, Welwyn, Herts, U.K. | lld:pubmed |
| pubmed-article:7980429 | pubmed:publicationType | Journal Article | lld:pubmed |
