Segmental mobility in glycogen phosphorylaseb

János Matkó, Sándor Papp, József Hevessy, Péter Nagy, Béla Somogy

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The dynamics and structuredness of the pyridoxal 5′-phosphate-binding region in glycogen phosphorylate b (EC 2.4.1.1) has been investigated with different techniques of fluorescence spectroscopy. Fluorescence polarization data of the thermal Perrin plot indicate some mobility in the cofactor binding site, while the isothermic measurements (at 20°C, in high-viscosity solvents) demonstrate that the mobile unit carrying the emission oscillator is practically insensitive to the external viscosity. Characteristics of the thermal Perrin plots obtained for both native and reduced phosphorylate f can be interpreted either as a freely moving cofactor in a medium of high viscosity (0.3 P) or as the motion of a unit larger than a lysine-bonded pyridoxal 5′-phosphate in a medium with the viscosity of water. Data for acrylamide quenching and time-resolved fluorescence measurements suggest that the latter interpretation should be valid. These data also suggest a tightly packed microenvironment around the pyridoxal moiety.

Original languageEnglish
Pages (from-to)42-48
Number of pages7
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume747
Issue number1-2
DOIs
Publication statusPublished - Sep 14 1983

Keywords

  • (Rabbit skeletal muscle)
  • Bluorescnece spectroscopy
  • Glycogen phosphorylase b
  • Molecular flexibility
  • Pyridoxal phosphate binding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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