pubmed-article:8035456 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8035456 | lifeskim:mentions | umls-concept:C0018364 | lld:lifeskim |
pubmed-article:8035456 | lifeskim:mentions | umls-concept:C0678595 | lld:lifeskim |
pubmed-article:8035456 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
pubmed-article:8035456 | lifeskim:mentions | umls-concept:C1504308 | lld:lifeskim |
pubmed-article:8035456 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:8035456 | pubmed:dateCreated | 1994-8-18 | lld:pubmed |
pubmed-article:8035456 | pubmed:abstractText | The cis conformation of the 38-39 peptide bond of ribonuclease T1 is retained after the replacement of cis Pro39 by an alanine residue. This conformation is demonstrated by the presence of a NOESY cross-peak in the NMR spectrum between the C alpha protons of Tyr38 and Ala39 in the Pro39-->Ala variant. The presence of this non-prolyl cis peptide bond explains the retention of the catalytic activity, the strong decrease in stability and the changes in the folding mechanism that were observed after the Pro39-->Ala mutation in ribonuclease T1. We suggest that a cis peptide bond is retained in a protein after the substitution of a cis proline at positions, where a trans bond would destabilize the protein more strongly than a non-prolyl peptide bond in the energetically unfavourable cis conformation. | lld:pubmed |
pubmed-article:8035456 | pubmed:language | eng | lld:pubmed |
pubmed-article:8035456 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8035456 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8035456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8035456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8035456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8035456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8035456 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8035456 | pubmed:month | Jul | lld:pubmed |
pubmed-article:8035456 | pubmed:issn | 0022-2836 | lld:pubmed |
pubmed-article:8035456 | pubmed:author | pubmed-author:SchmidF XFX | lld:pubmed |
pubmed-article:8035456 | pubmed:author | pubmed-author:RöschPP | lld:pubmed |
pubmed-article:8035456 | pubmed:author | pubmed-author:MayrL MLM | lld:pubmed |
pubmed-article:8035456 | pubmed:author | pubmed-author:WillboldDD | lld:pubmed |
pubmed-article:8035456 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8035456 | pubmed:day | 22 | lld:pubmed |
pubmed-article:8035456 | pubmed:volume | 240 | lld:pubmed |
pubmed-article:8035456 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8035456 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8035456 | pubmed:pagination | 288-93 | lld:pubmed |
pubmed-article:8035456 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:8035456 | pubmed:meshHeading | pubmed-meshheading:8035456-... | lld:pubmed |
pubmed-article:8035456 | pubmed:meshHeading | pubmed-meshheading:8035456-... | lld:pubmed |
pubmed-article:8035456 | pubmed:meshHeading | pubmed-meshheading:8035456-... | lld:pubmed |
pubmed-article:8035456 | pubmed:meshHeading | pubmed-meshheading:8035456-... | lld:pubmed |
pubmed-article:8035456 | pubmed:meshHeading | pubmed-meshheading:8035456-... | lld:pubmed |
pubmed-article:8035456 | pubmed:meshHeading | pubmed-meshheading:8035456-... | lld:pubmed |
pubmed-article:8035456 | pubmed:meshHeading | pubmed-meshheading:8035456-... | lld:pubmed |
pubmed-article:8035456 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:8035456 | pubmed:articleTitle | Generation of a non-prolyl cis peptide bond in ribonuclease T1. | lld:pubmed |
pubmed-article:8035456 | pubmed:affiliation | Laboratorium für Biochemie, Universität Bayreuth, Germany. | lld:pubmed |
pubmed-article:8035456 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8035456 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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