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Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H1⁰, Its carboxyl domain (H1⁰-C) or globular domain (H1⁰-G) to B-DNA.

ABSTRACT: Linker histones (H1) are the basic proteins in higher eukaryotes that are responsible for the final condensation of chromatin. In contrast to the nucleosome core histone proteins, the role of H1 in compacting DNA is not clearly understood. In this study ITC was used to measure the binding constant, enthalpy change, and binding site size for the interactions of H1⁰, or its C-terminal (H1⁰-C) and globular (H1⁰-G) domains to highly polymerized calf-thymus DNA at temperatures from 288 K to 308 K. Heat capacity changes, ΔC_p, for these same H1⁰ binding interactions were estimated from the temperature dependence of the enthalpy changes. The enthalpy changes for binding H1⁰, H1⁰-C, or H1⁰-G to CT-DNA are all en

SUBMITTER: Machha VR

PROVIDER: S-EPMC5645174 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Dataset Information

Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H1⁰, Its carboxyl domain (H1⁰-C) or globular domain (H1⁰-G) to B-DNA.

OmicsDI is part of the ELIXIR infrastructure

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Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H10, Its carboxyl domain (H10-C) or globular domain (H10-G) to B-DNA.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H1⁰, Its carboxyl domain (H1⁰-C) or globular domain (H1⁰-G) to B-DNA.