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Thermal denaturation of chromatin and lysine copolymer–DNA complexes. Effects of ethylene glycol
Author(s) -
Schwartz Arnold M.,
Fasman Gerald D.
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180503
Subject(s) - hyperchromicity , chromatin , ethylene glycol , chemistry , dna , denaturation (fissile materials) , ethylene , melting temperature , polymer chemistry , copolymer , biophysics , crystallography , biochemistry , polymer , organic chemistry , catalysis , materials science , nuclear chemistry , biology , composite material
Chromatin was thermally denatured in the presence and absence of 1 M ethylene glycol using a technique whereby both the hyperchromism and ellipticity are monitored simultaneously. Model complexes containing poly( L ‐Lys) or poly( L ‐Lys, L ‐Ala, Gly) and DNA were similarly melted in order to assist in interpreting the chromatin results. In both cases a general pattern emerged whereby ethylene glycol perturbed the resultant melting profile, showing increased hyperchromicity, ellipticity, and premelt slope. In addition, ethylene glycol destabilizes and reduces the high melting region of polypeptide‐bound DNA and the extent of higher ordered structure in model complexes and chromatin. These results emphasize the importance of hydrophobic forces in polypeptide–polypeptide and polypeptide–DNA interactions.