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Interaction of a tryptophan‐containing peptide with chromatin core particles
Author(s) -
Colot Vincent,
Toulme Jean-Jacques,
Helene Claude
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80319-1
Subject(s) - chemistry , stacking , tryptophan , indole test , dna , tetrapeptide , nucleic acid , peptide , fluorescence , peptide nucleic acid , chromatin , residue (chemistry) , histone , fluorescence spectroscopy , nucleosome , biophysics , stereochemistry , biochemistry , organic chemistry , amino acid , biology , physics , quantum mechanics
The binding of a tetrapeptide lysyltryptophylglycyllysine to nucleosome core particles has been investigated using UV absorption and fluorescence spectroscopy. Modifications of the absorption spectra and fluorescence quenching of the tryptophyl residue are consistent with stacking between the indole ring and nucleic acid bases. Therefore DNA interactions with histones do not prevent stacking of the tryptophyl residue with nucleic acid bases in the peptide—core particle complexes. The number of peptide binding sites is reduced to half that of naked DNA.