Open AccessAn Investigation of the Conformational Changes of Histone F2b by High Resolution Nuclear Magnetic Resonance
Author(s) -
Boublík Miloslav,
Bradbury E. Morton,
CraneRobinson Colyn,
Johns Ernest W.
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb01147.x
Subject(s) - ionic strength , chemistry , polypeptide chain , conformational change , histone , biophysics , nuclear magnetic resonance , ionic bonding , crystallography , biochemistry , ion , enzyme , biology , physics , organic chemistry , dna , aqueous solution
The recent sequence determination of histone F2b has allowed a detailed nuclear magnetic resonance study of the conformational changes and interactions of this protein with (a) increasing ionic strength, (b) increasing concentration and (c) change of pH. In all cases it has been found that a specific region of the polypeptide chain is involved in the induced changes: with increasing ionic strength the changes and interaction can be located in the segment of the polypeptide chain from residues 60 to 102; part of this segment is also involved in the specific aggregation that occurs on increasing the concentrations, while for the pH induced changes the same segment together with additional residues at each end is involved in the observed changes.