ISSN:
0006-3525
Keywords:
DNA recognition
;
nucleosome recognition
;
deformation
;
DNA-binding protein
;
conformational fluctuations
;
protein-DNA complexes
;
histone octamer
;
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The affinity of a DNA sequence for the histone octamer in a core nucleosome depends on the intrinsic flexibility of the DNA. This parameter can be affected both by the sequence-dependent conformational preferences of individual base steps and by the nature and location of the exocyclic groups of the DNA bases. By adopting highly preferred conformations particular types of base step can influence the rotational positioning of the DNA on the surface of the histone octamer. The asymmetry of the next higher order of chromatin structure is determined in part by the asymmetric binding of the globular domain of histone H5 to the core nucleosome. © 1998 John Wiley & Sons, Inc. Biopoly 44: 423-433 1997
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
