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| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C0040688 | lld:lifeskim |
| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C0596957 | lld:lifeskim |
| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C0028580 | lld:lifeskim |
| pubmed-article:2320585 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:2320585 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:2320585 | pubmed:dateCreated | 1990-5-4 | lld:pubmed |
| pubmed-article:2320585 | pubmed:abstractText | A restrained molecular dynamics simulation approach that explicitly includes the effect of the surrounding solvent molecules is applied to the NMR determination of the conformations of the B-loop fragments of human transforming growth factor alpha and epidermal growth factor. Backbone interproton distance restraints are obtained by using two-dimensional rotating frame nuclear Overhauser effect spectroscopy (ROESY). The simulations are carried out both in "vacuum" and in "water." The results are discussed in terms of the energetics, agreement with the NMR distances, and the flexibility of the peptides. | lld:pubmed |
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| pubmed-article:2320585 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2320585 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2320585 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2320585 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2320585 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2320585 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2320585 | pubmed:author | pubmed-author:FerrettiJ AJA | lld:pubmed |
| pubmed-article:2320585 | pubmed:author | pubmed-author:BrooksB RBR | lld:pubmed |
| pubmed-article:2320585 | pubmed:author | pubmed-author:RAOS SSS | lld:pubmed |
| pubmed-article:2320585 | pubmed:author | pubmed-author:SyiJ LJL | lld:pubmed |
| pubmed-article:2320585 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2320585 | pubmed:volume | 87 | lld:pubmed |
| pubmed-article:2320585 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2320585 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2320585 | pubmed:pagination | 2818-22 | lld:pubmed |
| pubmed-article:2320585 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2320585 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2320585 | pubmed:articleTitle | Solution conformations of the B-loop fragments of human transforming growth factor alpha and epidermal growth factor by 1H nuclear magnetic resonance and restrained molecular dynamics. | lld:pubmed |
| pubmed-article:2320585 | pubmed:affiliation | Laboratory of Chemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892. | lld:pubmed |
| pubmed-article:2320585 | pubmed:publicationType | Journal Article | lld:pubmed |
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