Linked Life Data

16028948

Source:http://linkedlifedata.com/resource/pubmed/id/16028948

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
2005-7-20
pubmed:abstractText
The conformational space of tryptamine has been thoroughly investigated using rotationally resolved laser-induced fluorescence spectroscopy. Six conformers could be identified on the basis of the inertial parameters of several deuterated isotopomers. Upon attaching a single water molecule, the conformational space collapses into a single conformer. For the hydrogen-bonded water cluster, this conformer is identified unambiguously as tryptamine A. In the complex, the water molecule acts as proton donor with respect to the amino group. An additional interaction with one of the aromatic C-H bonds selectively stabilizes the observed conformer more than all other conformers. Ab initio calculations confirm much larger energy differences between the conformers of the water complex than between those of the monomers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10356-64
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Structural selection by microsolvation: conformational locking of tryptamine.
pubmed:affiliation
Institut für Physikalische Chemie, Heinrich-Heine-Universität, D-40225 Düsseldorf, Germany. mschmitt@uni-duesseldorf.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't