Linked Life Data

3134060

Source:http://linkedlifedata.com/resource/pubmed/id/3134060

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-8-18
pubmed:abstractText
Electronic transition properties of indole perturbed by its environment were calculated by use of quantum-mechanical semi-empirical numerical methods. The environment was represented by a discrete set of charges placed at different positions around the indole ring. Wavelength shifts and transition intensity changes in indole were evaluated for several, specifically modeled geometries of external charges. This methodology was employed to estimate the extent of spectroscopic changes induced by small nonprotein polar species on the Trp-59 residue in the anisotropic environment of the protein ribonuclease T1. The geometry of the residue environment was obtained from dynamically equilibrated X-ray crystallographic data of the protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
341-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Electronic transitions in molecules in static external fields. I. Indole and Trp-59 in ribonuclease T1.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Mayo Graduate School, Mayo Foundation, Rochester, MN 55905.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't