| pubmed-article:1392568 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C0162807 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C0231881 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C1516050 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C2348867 | lld:lifeskim |
| pubmed-article:1392568 | lifeskim:mentions | umls-concept:C0063602 | lld:lifeskim |
| pubmed-article:1392568 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1392568 | pubmed:dateCreated | 1992-11-10 | lld:pubmed |
| pubmed-article:1392568 | pubmed:abstractText | A 500 MHz 2D 1H NMR study of recombinant insect defensin A is reported. This defense protein of 40 residues contains 3 disulfide bridges, is positively charged and exhibits antibacterial properties. 2D NMR maps of recombinant defensin A were fully assigned and secondary structure elements were localized. The set of NOE connectivities, 3JNH-alpha H coupling constants as well as 1H/2H exchange rates and delta delta/delta T temperature coefficients of NH protons strongly support the existence of an alpha-helix (residues 14-24) and of an antiparallel beta-sheet (residues 27-40). Models of the backbone folding were generated by using the DISMAN program and energy refined by using the AMBER program. This was done on the basis of: (i) 133 selected NOEs, (ii) 21 dihedral restraints from 3JNH-alpha H coupling constants, (iii) 12 hydrogen bonds mostly deduced from 1H/2H exchange rates or temperature coefficients, in addition to 9 initial disulfide bridge covalent constraints. The two secondary structure elements and the two bends connecting them involve approximately 70% of the total number of residues, which impose some stability in the C-terminal part of the molecule. The remaining N-terminal fragment forms a less well defined loop. This spatial organization, in which a beta-sheet is linked to an alpha-helix by two disulfide bridges and to a large loop by a third disulfide bridge, is rather similar to that found in scorpion charybdotoxin and seems to be partly present in several invertebrate toxins. | lld:pubmed |
| pubmed-article:1392568 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1392568 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1392568 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1392568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1392568 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1392568 | pubmed:month | May | lld:pubmed |
| pubmed-article:1392568 | pubmed:issn | 0925-2738 | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:PtakMM | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:LegrainMM | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:ReichhartJ... | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:VovelleFF | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:HoffmannJ AJA | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:AchstetterTT | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:BonnatJ LJL | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:KeppiEE | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:BonmatinJ MJM | lld:pubmed |
| pubmed-article:1392568 | pubmed:author | pubmed-author:GalletXX | lld:pubmed |
| pubmed-article:1392568 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1392568 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:1392568 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1392568 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1392568 | pubmed:pagination | 235-56 | lld:pubmed |
| pubmed-article:1392568 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1392568 | pubmed:meshHeading | pubmed-meshheading:1392568-... | lld:pubmed |
| pubmed-article:1392568 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1392568 | pubmed:articleTitle | Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding. | lld:pubmed |
| pubmed-article:1392568 | pubmed:affiliation | Centre de Biophysique Moléculaire (CNRS), Orléans, France. | lld:pubmed |
| pubmed-article:1392568 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1392568 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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