An Investigation of the Conformational Changes of Histone F2b by High Resolution Nuclear Magnetic Resonance

Abstract

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. Copyright © 1970, Wiley Blackwell. All rights reserved