journal cover

Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability

Biochemistry

May 2, 1995

V KarantzaEvangelos N Moudrianakis

Abstract

The thermal stability of the core histone dimer H2A-H2B has been studied by high-sensitivity differential scanning calorimetry and circular dichroism spectroscopy. The unfolding transition temperature of the 28 kDa H2A-H2B dimer increases as a function of both the ionic strength of the ...read more

Mentioned in this Paper

Thermodynamics
Macromolecular Compounds
Histone antigen
Aggregation
Dimer
Denaturation
Calorimetry, Differential Scanning
Circular Dichroism, Vibrational
Protein Folding, Globular
Spectrum Analysis
Paper Details
References
  • References22
  • Citations28
123
  • References22
  • Citations28
123

Related Papers

© 2020 Meta ULC. All rights reserved

Thermodynamic studies of the core histones: ionic strength and pH dependence of H2A-H2B dimer stability

Biochemistry

May 2, 1995

V KarantzaEvangelos N Moudrianakis

PMID: 7727455

DOI: 10.1021/bi00017a028

Abstract

The thermal stability of the core histone dimer H2A-H2B has been studied by high-sensitivity differential scanning calorimetry and circular dichroism spectroscopy. The unfolding transition temperature of the 28 kDa H2A-H2B dimer increases as a function of both the ionic strength of the ...read more

Mentioned in this Paper

Thermodynamics
Macromolecular Compounds
Histone antigen
Aggregation
Dimer
Denaturation
Calorimetry, Differential Scanning
Circular Dichroism, Vibrational
Protein Folding, Globular
Spectrum Analysis
Paper Details
References
  • References22
  • Citations28
123
  • References22
  • Citations28
123
/papers/thermodynamic-studies-of-the-core-histones-ionic/7727455