Linked Life Data

758326

Source:http://linkedlifedata.com/resource/pubmed/id/758326

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-2-21
pubmed:abstractText
Oligopeptides containing tyrosyl, lysyl, and alanyl residues bind to polynucleotides and nucleic acids as shown by proton magnetic resonance, fluorescence spectroscopy, and difference absorption spectroscopy. Proton magnetic resonance data indicate that stacking of tyrosyl residues with nucleic acid bases takes place only in single-stranded structures (such as poly(A) or denatured DNA). Stacking interactions lead to a quenching of tyrosine fluorescence. However, the tyrosyl fluorescence of the peptides is quenched in their complexes with both single-stranded and double-stranded nucleic acids. A comparison of the behavior of homologous peptides containing Tyr, methoxytyrosine, and Phe leads to the conclusion that hydrogen bonding of tyrosine with bases or phosphates is not involved in the investigated complexes. An energy transfer mechanism from tyrosine to nucleic acid bases is proposed to account for fluorescence quenching in oligopeptide complexes with double-stranded DNAs. Due to the specificity of its stacking interaction for single-stranded nucleic acid structures, tyrosine might be involved through such interactions in the selective recognition of single strands by proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-82
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
The role of tyrosine in the association of proteins and nucleic acids. Specific recognition of single-stranded nucleic acids by tyrosine-containing peptides.
pubmed:publicationType
Journal Article