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Investigation of the complexes of EcoRI endonuclease with decanucleotides containing canonical and modified recognition sequences using fluorescence and optical detection of magnetic resonance spectroscopy.

Publication ,  Journal Article
Jhon, NI; Casas-Finet, JR; Maki, AH; Modrich, P
Published in: Biochim Biophys Acta
February 28, 1988

The binding of EcoRI endonuclease to the oligonucleotides d(GCGAATTCGC) and d(GCGAA) (5BrdU) (5BrdU) d(CGC) has been investigated to determine whether stacking interactions occur between tryptophan residues and the DNA bases. Fluorescence binding isotherms show that the decamer containing the canonical and that containing the modified recognition sequence bind with comparable affinity. Optically detected magnetic resonance spectra show limited perturbations of the Trp zero-field splitting parameters, which are assigned to electrical field effects. No evidence for Trp stacking interactions has been found.

Duke Scholars

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

February 28, 1988

Volume

949

Issue

2

Start / End Page

189 / 194

Location

Netherlands

Related Subject Headings

  • Tryptophan
  • Spectrometry, Fluorescence
  • Protein Binding
  • Magnetic Resonance Spectroscopy
  • In Vitro Techniques
  • Deoxyribonuclease EcoRI
  • DNA-Binding Proteins
  • DNA Restriction Enzymes
  • DNA
  • Binding Sites
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Jhon, N. I., Casas-Finet, J. R., Maki, A. H., & Modrich, P. (1988). Investigation of the complexes of EcoRI endonuclease with decanucleotides containing canonical and modified recognition sequences using fluorescence and optical detection of magnetic resonance spectroscopy. Biochim Biophys Acta, 949(2), 189–194. https://doi.org/10.1016/0167-4781(88)90082-6
Jhon, N. I., J. R. Casas-Finet, A. H. Maki, and P. Modrich. “Investigation of the complexes of EcoRI endonuclease with decanucleotides containing canonical and modified recognition sequences using fluorescence and optical detection of magnetic resonance spectroscopy.Biochim Biophys Acta 949, no. 2 (February 28, 1988): 189–94. https://doi.org/10.1016/0167-4781(88)90082-6.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

February 28, 1988

Volume

949

Issue

2

Start / End Page

189 / 194

Location

Netherlands

Related Subject Headings

  • Tryptophan
  • Spectrometry, Fluorescence
  • Protein Binding
  • Magnetic Resonance Spectroscopy
  • In Vitro Techniques
  • Deoxyribonuclease EcoRI
  • DNA-Binding Proteins
  • DNA Restriction Enzymes
  • DNA
  • Binding Sites