| pubmed-article:2611235 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C1511726 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C0332462 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C0870071 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C1523987 | lld:lifeskim |
| pubmed-article:2611235 | lifeskim:mentions | umls-concept:C0132320 | lld:lifeskim |
| pubmed-article:2611235 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:2611235 | pubmed:dateCreated | 1990-3-14 | lld:pubmed |
| pubmed-article:2611235 | pubmed:abstractText | The structure of neutrophil peptide 5 in solution has recently been reported (Pardi et al., 1988). The structure determination was accomplished by using a distance geometry algorithm and 107 interproton distance constraints obtained from 2D NMR data. In each of the eight independent solutions to the distance geometry equations, the overall fold of the polypeptide backbone was identical and the root mean square (rms) deviation between backbone atoms of the superimposed structures was small (approximately 2.4 A). In this paper we report additional NP-5 structures obtained by using a new structure generation algorithm: a Monte Carlo search in torsion angle space. These structures have a large rms backbone deviation from the distance geometry structures (approximately 5.0 A). The backbone topologies differ in significant respects from the distance geometry structures and from each other. Structures are found that are pseudo mirror images of part or all of the fold corresponding to that first obtained with the distance geometry procedure. For small proteins, the problem of distinguishing the correct structure among pseudo mirror images is likely to be greater than previously recognized. When a set of test distance constraints constructed from a novel Monte Carlo structure is used as input in the distance geometry algorithm, the fold of the resulting structure does not correspond to that of the target. The results also demonstrate that the previously accepted criteria (the magnitude of the rms deviation between multiple solutions of the distance geometry equations) for defining the accuracy and precision of a peptide structure generated from NMR data are inadequate. An energetic analysis of structures corresponding to the different folding topologies has been carried out. The molecular mechanics energies obtained by minimization and molecular dynamics refinement provide sufficient information to eliminate certain alternative structures. On the basis of a careful comparison of the different trial structures with the experimental data, it is concluded that the NP-5 peptide fold which was originally reported is most consistent with the data. An alternative fold corresponding to structures with low energies and small total distance violations is ruled out because for this fold predicted NOEs are not observed experimentally. | lld:pubmed |
| pubmed-article:2611235 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2611235 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2611235 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2611235 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2611235 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2611235 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2611235 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2611235 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2611235 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2611235 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2611235 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2611235 | pubmed:author | pubmed-author:LevyR MRM | lld:pubmed |
| pubmed-article:2611235 | pubmed:author | pubmed-author:PardoKK | lld:pubmed |
| pubmed-article:2611235 | pubmed:author | pubmed-author:KitchenD BDB | lld:pubmed |
| pubmed-article:2611235 | pubmed:author | pubmed-author:BassolinoD... | lld:pubmed |
| pubmed-article:2611235 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2611235 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:2611235 | pubmed:volume | 28 | lld:pubmed |
| pubmed-article:2611235 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2611235 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2611235 | pubmed:pagination | 9361-72 | lld:pubmed |
| pubmed-article:2611235 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:meshHeading | pubmed-meshheading:2611235-... | lld:pubmed |
| pubmed-article:2611235 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2611235 | pubmed:articleTitle | Solution structures of proteins from NMR data and modeling: alternative folds for neutrophil peptide 5. | lld:pubmed |
| pubmed-article:2611235 | pubmed:affiliation | Department of Chemistry, Rutgers University, New Brunswick, New Jersey 08903. | lld:pubmed |
| pubmed-article:2611235 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2611235 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2611235 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:100009136 | entrezgene:pubmed | pubmed-article:2611235 | lld:entrezgene |
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