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

Biochemistry

May 2, 1995

V KarantzaEvangelos N Moudrianakis

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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
Histone H7
Denaturation
Circular Dichroism, Vibrational
Protein Folding, Globular
Circular Dichroism
Metazoa
Histone antigen
Aggregation
Hydrogen-Ion Concentration
Paper Details
References
  • References22
  • Citations28
  • References22
  • Citations28
123

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
Histone H7
Denaturation
Circular Dichroism, Vibrational
Protein Folding, Globular
Paper Details
References
  • References22
  • Citations28
  • References22
  • Citations28
123

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