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pubmed-article:8035456pubmed:abstractTextThe 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
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pubmed-article:8035456pubmed:pagination288-93lld:pubmed
pubmed-article:8035456pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:8035456pubmed:articleTitleGeneration of a non-prolyl cis peptide bond in ribonuclease T1.lld:pubmed
pubmed-article:8035456pubmed:affiliationLaboratorium für Biochemie, Universität Bayreuth, Germany.lld:pubmed
pubmed-article:8035456pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8035456pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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