| pubmed-article:964248 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:964248 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
| pubmed-article:964248 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:964248 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:964248 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:964248 | lifeskim:mentions | umls-concept:C0019649 | lld:lifeskim |
| pubmed-article:964248 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:964248 | pubmed:dateCreated | 1976-11-21 | lld:pubmed |
| pubmed-article:964248 | pubmed:abstractText | Spectroscopic studies (nuclear magnetic resonance, circular dichroism and infrared) have been carried out on chicken erythrocyte histone H5 and on three peptides cleaved therefrom: 1-31, 32-197 and 58-197. It is shown that at ionic strengths above o.1M part of the H5 molecule takes up a globular conformation containing 14% alpha helix but no beta sheet structure. Several details of the circular dichroism and nuclear magnetic resonace spectra indicate that the globular region is located in the N-terminal half of the molecule and this proposal is supported by the observation that the peptide 32-197 is largely incapable of folding and the peptide 59-197 is completely incapable of folding. Structural similarities and differences between histone H5 and histone H1 are discussed. | lld:pubmed |
| pubmed-article:964248 | pubmed:language | eng | lld:pubmed |
| pubmed-article:964248 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:964248 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:964248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:964248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:964248 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:964248 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:964248 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:964248 | pubmed:author | pubmed-author:BradburyE MEM | lld:pubmed |
| pubmed-article:964248 | pubmed:author | pubmed-author:Crane-Robinso... | lld:pubmed |
| pubmed-article:964248 | pubmed:author | pubmed-author:GarelAA | lld:pubmed |
| pubmed-article:964248 | pubmed:author | pubmed-author:DauneMM | lld:pubmed |
| pubmed-article:964248 | pubmed:author | pubmed-author:ChampagneMM | lld:pubmed |
| pubmed-article:964248 | pubmed:author | pubmed-author:KovacsA MAM | lld:pubmed |
| pubmed-article:964248 | pubmed:author | pubmed-author:DancyS ESE | lld:pubmed |
| pubmed-article:964248 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:964248 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:964248 | pubmed:volume | 67 | lld:pubmed |
| pubmed-article:964248 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:964248 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:964248 | pubmed:pagination | 379-88 | lld:pubmed |
| pubmed-article:964248 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:964248 | pubmed:meshHeading | pubmed-meshheading:964248-A... | lld:pubmed |
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| pubmed-article:964248 | pubmed:meshHeading | pubmed-meshheading:964248-M... | lld:pubmed |
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| pubmed-article:964248 | pubmed:meshHeading | pubmed-meshheading:964248-C... | lld:pubmed |
| pubmed-article:964248 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:964248 | pubmed:articleTitle | Structural studies of chicken erythrocyte histone H5. | lld:pubmed |
| pubmed-article:964248 | pubmed:publicationType | Journal Article | lld:pubmed |
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