Linked Life Data

2489103

Source:http://linkedlifedata.com/resource/pubmed/id/2489103

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1991-5-29
pubmed:abstractText
Conformational energy computations on the 1-aminocyclopropane-1-carboxylic acid mono-, di-, and tripeptide amides, Ac-(Ac3c)n-NHMe (n = 1-3), indicate that this C alpha, alpha-dialkylated, cyclic alpha-amino acid residue is conformally restricted and that type-I(I') beta-bends and distorted 3(10)-helices are particularly stable conformations for the di- and tripeptide amides, respectively. The results of the theoretical analysis are in agreement with those obtained in an i.r. absorption and 1H n.m.r. investigation in chloroform solution of Ac3c-rich tri- and tetrapeptide esters. A comparison is also made with the conclusions extracted from our previous work on peptides rich in Aib (alpha-aminoisobutyric acid), Ac5c (1-aminocyclopentane-1-carboxylic acid), and Ac6c (1-aminocyclohexane-1-carboxylic acid).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0141-8130
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
N
pubmed:pagination
345-52
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Structural versatility of peptides containing C alpha, alpha-dialkylated glycines: conformational energy computations, i.r. absorption and 1H n.m.r. analysis of 1-aminocyclopropane-1-carboxylic acid homopeptides.
pubmed:affiliation
Department of Organic Chemistry, University of Padua, Italy.
pubmed:publicationType
Journal Article