Linked Life Data

8913855

Source:http://linkedlifedata.com/resource/pubmed/id/8913855

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-2-14
pubmed:abstractText
The potential energy surface of the phi [NHCO] delta Ala dipeptide has been computed using ab initio quantum mechanical calculations at different theoretical levels. Three degenerate minima were found and characterized. The most favoured conformation is stabilized by an intramolecular hydrogen bonding interaction. The other two minima correspond to helical and malonamide-like conformations, being 4.6 kcal/mol and 6.9 kcal/mol less stable than the lowest energy conformation, respectively. Influence of solvent effects on the relative stabilities of the different conformations have been accounted using SCRF calculations. Two implicit solvent models have been considered: water and CCl4. The results indicate that in the both cases the conformation with an intramolecular hydrogen bonding interaction retains its lowest energy.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0739-1102
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-9
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Effects of the phi[NHCO] retromodification on dehydroalanine dipeptide.
pubmed:affiliation
Department d'Enginyeria Química, E.T.S.I.I.B., Universitat Politècnica de Catalunya, Barcelona, Spain.
pubmed:publicationType
Journal Article