| pubmed-article:204332 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C0439801 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C0008813 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:204332 | lifeskim:mentions | umls-concept:C0111958 | lld:lifeskim |
| pubmed-article:204332 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:204332 | pubmed:dateCreated | 1978-5-17 | lld:pubmed |
| pubmed-article:204332 | pubmed:abstractText | gp32 I is a protein with a molecular weight of 27 000. It is obtained by limited hydrolysis of T4 gene 32 coded protein, which is one of the DNA melting proteins. gp32 I itself appears to be also a melting protein. It denatures poly[d(A-T)].poly[d(A-T)] and T4 DNA at temperatures far (50-60 degrees C) below their regular melting temperatures. Under similar conditions gp32 I will denature poly[d(A-T).poly[d(A-T)] at temperatures approximately 12 degrees C lower than those measured for the intact gp32 denaturation. For T4 DNA gp32 shows no melting behavior while gp32 I shows considerable denaturation (i.e., hyperchromicity) even at 1 degree C. In this paper the denaturation of poly[d(A-T)].poly[d(A-T)] and T4 DNA by gp32 I is studied by means of circular dichroism. It appears that gp32 I forms a complex with poly[d(A-T)]. The conformation of the polynucleotide in the complex is equal to that of one strand of the double-stranded polymer in 6 M LiCl. In the gp32 I DNA complex formed upon denaturation of T4 DNA, the single-stranded DNA molecule has the same conformation as one strand of the double-strand T4 DNA molecule in the C-DNA conformation. | lld:pubmed |
| pubmed-article:204332 | pubmed:language | eng | lld:pubmed |
| pubmed-article:204332 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:204332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:204332 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:204332 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:204332 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:204332 | pubmed:author | pubmed-author:MoiseHH | lld:pubmed |
| pubmed-article:204332 | pubmed:author | pubmed-author:HosodaJJ | lld:pubmed |
| pubmed-article:204332 | pubmed:author | pubmed-author:MaestreM FMF | lld:pubmed |
| pubmed-article:204332 | pubmed:author | pubmed-author:GreveJJ | lld:pubmed |
| pubmed-article:204332 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:204332 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:204332 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:204332 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:204332 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:204332 | pubmed:pagination | 893-8 | lld:pubmed |
| pubmed-article:204332 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:204332 | pubmed:meshHeading | pubmed-meshheading:204332-P... | lld:pubmed |
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| pubmed-article:204332 | pubmed:meshHeading | pubmed-meshheading:204332-D... | lld:pubmed |
| pubmed-article:204332 | pubmed:meshHeading | pubmed-meshheading:204332-N... | lld:pubmed |
| pubmed-article:204332 | pubmed:meshHeading | pubmed-meshheading:204332-P... | lld:pubmed |
| pubmed-article:204332 | pubmed:meshHeading | pubmed-meshheading:204332-P... | lld:pubmed |
| pubmed-article:204332 | pubmed:meshHeading | pubmed-meshheading:204332-D... | lld:pubmed |
| pubmed-article:204332 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:204332 | pubmed:articleTitle | Circular dichroism studies of the interaction of a limited hydrolysate of T4 gene 32 protein with T4 DNA and poly[d(A-T)].poly[d(A-T)]. | lld:pubmed |
| pubmed-article:204332 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:204332 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:204332 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:204332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:204332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:204332 | lld:pubmed |
