A proton magnetic relaxation study of methaemoproteins bound to monodisperse polystyrene latex particles

Bojan Benko, Stanimir Vuk-Pavlovic, Gjuro Dezelic, Sinisa Marićić

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

The influence of the binding of methaemoproteins to latex particles with respect to protein conformation was examined using the longitudinal magnetic relaxation rates of solvent protons. The temperature dependences of the paramagnetically induced molar relaxation rates in bound metmyoglobin samples as well as their absolute values suggest an opening of the haem-pocket. The decrease of the same parameter for the immobilized methaemoglobin points to a smaller haem-pocket accessibility with respect to that in the solution. The changes of the haem-pocket structure found for both methaemoproteins support the idea that proteins change their conformation by their binding to the solid surface, although in opposite ways.

Original languageEnglish (US)
Pages (from-to)444-451
Number of pages8
JournalJournal of Colloid And Interface Science
Volume52
Issue number3
DOIs
StatePublished - Sep 1975

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Surfaces, Coatings and Films
  • Colloid and Surface Chemistry

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