Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H1 0 , Its carboxyl domain (H1 0 -C) or globular domain (H1 0 -G) to B-DNA-Reference-Cited by-同舟云学术

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Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H1 0 , Its carboxyl domain (H1 0 -C) or globular domain (H1 0 -G) to B-DNA

Published:2017-12 Issue: Volume:12 Page:158-165
ISSN:2405-5808
Container-title:Biochemistry and Biophysics Reports
language:en
Short-container-title:Biochemistry and Biophysics Reports

Author:

Machha V.R.,Mikek C.G.,Wellman S.,Lewis E.A.

Funder

National Science Foundation

DoEd GAANN

Publisher

Elsevier BV

Subject

Biochemistry,Biophysics

Reference34 articles.

1. Histone H1 and its isoforms: contribution to chromatin structure and function;Happel;Gene,2009

2. Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin;Orrego;BMC Biol.,2007

3. Analysis of the charge distribution in the C-terminal region of histone H1 as related to its interaction with DNA;Subirana;Biopolymers,1990

4. Calorimetric studies of the interactions of linker histone H1(0) and its carboxyl (H1(0)-C) and globular (H1(0)-G) domains with calf-thymus DNA;Machha,2013

5. Binding of histone H1 to DNA is described by an allosteric model;Mamoon;Biopolymers,2004

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1. Approach to the Investigation of Nucleosome Structure by Using the Highly Emissive Nucleobase th dG–tC FRET Pair;Chemistry – A European Journal;2018-10-24

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