Salt effects on bacteriophage T7-I.

K. Tóth, G. Rontó

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The thermal denaturation as a measure of the structural stability of the nucleoprotein in bacteriophage T7 has been studied in dependence of the ionic environment. Optical density and circular dichroism melting curves measured at wavelengths characterizing either the DNA or protein conformational changes were compared to identify different steps of the denaturation and to follow the effect of the ions. Monovalent salts strengthen the helical structure of intraphage DNA logarithmically in the way as they do in the case of isolated double-stranded DNA. Mg2+ and Ca2+ at very low concentrations stabilize the DNA helicity. Higher divalent ion concentrations decrease the stability of the double helix because of the repulsive ionic interactions. The high structural sensitivity of DNA in the presence of Mg2+ and Ca2+ in this "in situ" environment can be related to the biological role of these ions.

Original languageEnglish
Pages (from-to)59-66
Number of pages8
JournalPhysiological Chemistry and Physics and Medical NMR
Volume19
Issue number1
Publication statusPublished - 1987

Fingerprint

Bacteriophage T7
Bacteriophages
Salts
DNA
Denaturation
Ions
Nucleoproteins
Density (optical)
Dichroism
Circular Dichroism
Freezing
Melting
Hot Temperature
Wavelength
Proteins

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Physiology
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Radiological and Ultrasound Technology

Cite this

Salt effects on bacteriophage T7-I. / Tóth, K.; Rontó, G.

In: Physiological Chemistry and Physics and Medical NMR, Vol. 19, No. 1, 1987, p. 59-66.

Research output: Contribution to journalArticle

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