|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1979-1-15
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|
pubmed:abstractText |
The base catalyzed ring closure in t-Boc-Asp-X beta-napthylamides was examined in a series of 2-peptide derivatives in which position X was occupied by the neutral and acidic amino acid residues that occur in proteins. Bulkiness and functional groups in the side chain of X have a major effect on the rate of cyclization, e.g. acidic groups slow down the formation of aminosuccinyl derivatives. Rate-enhancing effect can be observed in serine and threonine, while the side reaction is unexpectedly slow when X is methionine.
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|
pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0367-8377
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
12
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
69-74
|
|
pubmed:dateRevised |
2008-11-21
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|
pubmed:meshHeading |
|
|
pubmed:year |
1978
|
|
pubmed:articleTitle |
Side reactions in peptide synthesis. VII. Sequence dependence in the formation of aminosuccinyl derivatives from beta-benzyl-aspartyl peptides.
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|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|
