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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1994-8-18
|
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0022-2836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
22
|
| pubmed:volume |
240
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
288-93
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1994
|
| pubmed:articleTitle |
Generation of a non-prolyl cis peptide bond in ribonuclease T1.
|
| pubmed:affiliation |
Laboratorium für Biochemie, Universität Bayreuth, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|