| pubmed-article:2719660 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2719660 | lifeskim:mentions | umls-concept:C0205341 | lld:lifeskim |
| pubmed-article:2719660 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:2719660 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:2719660 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
| pubmed-article:2719660 | lifeskim:mentions | umls-concept:C2350166 | lld:lifeskim |
| pubmed-article:2719660 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2719660 | pubmed:dateCreated | 1989-6-20 | lld:pubmed |
| pubmed-article:2719660 | pubmed:abstractText | C hordein, a storage protein from barley grains, has an Mr of about 53,000, and consists predominantly of repeated octapeptides with a consensus sequence of Pro-Gln-Gln-Pro-Phe-Pro-Gln-Gln. Previously reported hydrodynamic and c.d. studies indicate the presence of beta-turns, the repetitive nature of which may lead to the formation of a loose spiral. In order to study these turns we have compared the structures of a synthetic peptide corresponding to the consensus repeat motif and total C hordein by using c.d. and Fourier-transform i.r. spectroscopy. The synthetic peptide exhibited spectra typical of beta I/III reverse turns when dissolved in trifluoroethanol at 22 degrees C and in water at 70 degrees C, but 'random-coil'-like spectra in water at 22 degrees C. The whole protein also showed increases in beta I/III reverse turns when dissolved in increasing concentrations of trifluoroethanol (50-100%, v/v) or heated in ethanol/water (7:3, v/v). Two cryogenic solvent systems were used to determine the c.d. spectra of the peptide and protein at temperatures down to -100 degrees C. Methanol/glycerol (9:1, v/v) and ethanediol/water (2:1, v/v) were selected as analogues of trifluoroethanol/water and water respectively. The peptide exhibited beta I/III-reverse-turn and 'random-coil'-like spectra in methanol/glycerol and ethanediol/water respectively at 22 degrees C, but a spectrum similar to that of a poly-L-proline II helix in both solvents at -100 degrees C. Similarly the proportion of this spectral type also increased when the whole protein was cooled in both solvents. These results indicate that a poly-L-proline II conformation at low temperatures is in equilibrium with a beta I/III-turn-rich conformation at higher temperatures. The latter conformation is also favoured in solvents of low dielectric constant such as trifluoroethanol. The 'random-coil'-like spectra exhibited by the protein and peptide in high-dielectric-constant solvents at room temperature may result from a mixture of the two conformations rather than from the random-coil state. | lld:pubmed |
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| pubmed-article:2719660 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2719660 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2719660 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2719660 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2719660 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2719660 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2719660 | pubmed:author | pubmed-author:DrakeA FAF | lld:pubmed |
| pubmed-article:2719660 | pubmed:author | pubmed-author:ShewryP RPR | lld:pubmed |
| pubmed-article:2719660 | pubmed:author | pubmed-author:TathamA SAS | lld:pubmed |
| pubmed-article:2719660 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2719660 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2719660 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:2719660 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2719660 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2719660 | pubmed:pagination | 471-6 | lld:pubmed |
| pubmed-article:2719660 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2719660 | pubmed:meshHeading | pubmed-meshheading:2719660-... | lld:pubmed |
| pubmed-article:2719660 | pubmed:meshHeading | pubmed-meshheading:2719660-... | lld:pubmed |
| pubmed-article:2719660 | pubmed:meshHeading | pubmed-meshheading:2719660-... | lld:pubmed |
| pubmed-article:2719660 | pubmed:meshHeading | pubmed-meshheading:2719660-... | lld:pubmed |
| pubmed-article:2719660 | pubmed:meshHeading | pubmed-meshheading:2719660-... | lld:pubmed |
| pubmed-article:2719660 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2719660 | pubmed:articleTitle | Conformational studies of a synthetic peptide corresponding to the repeat motif of C hordein. | lld:pubmed |
| pubmed-article:2719660 | pubmed:affiliation | Department of Biochemistry, A.F.R.C. Institute of Arable Crops Research, Rothamsted Experimental Station, Harpenden, Herts, U.K. | lld:pubmed |
| pubmed-article:2719660 | pubmed:publicationType | Journal Article | lld:pubmed |
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