Linked Life Data

18464982

Source:http://linkedlifedata.com/resource/pubmed/id/18464982

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2008-5-9
pubmed:abstractText
Using a database of 6166 experimental structures taken from the Protein Data Bank, we have studied pair interactions between planar residues (Phe, Tyr, His, Arg, Glu and Asp) in proteins, known as pi-pi interactions. On the basis of appropriate coordinates defining the mutual arrangement of two residues, we have calculated 2-D potentials of mean force aimed at determining the stability of the most probable structures for aromatic-aromatic, aromatic-cation and aromatic-anion bound pairs. Our analysis reveals the thermodynamic relevance and the ubiquity of stacked complexes in proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1463-9076
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2673-85
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Thermodynamics of stacking interactions in proteins.
pubmed:affiliation
Dipartimento di Chimica, Università di Firenze, Sesto Fiorentino, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't