Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filtering

Gennaro Esposito, Arthur M. Lesk, Henriette Molinari, Andrea Motta, Neri Niccolai, Annalisa Pastore

Research output: Contribution to journalArticle

Abstract

Soluble spin labels, which "bleach" the surface proton resonances of a protein to n.m.r. measurements, can provide useful information about protein conformation and dynamics. The use of the soluble nitroxide, TEMPOL, has been explored to show the correlation of the paramagnetic perturbations of protein two-dimensional n.m.r. data with proton exposure to the free radical in hen egg-white lysozyme. The results demonstrate that the nitroxide approaches the protein randomly, and that the extent of the observed paramagnetic effects reflects the native folding pattern of the protein. A correlation of spectral simplification with the known tertiary structure establishes the feasibility of new strategies for topological mapping of surface and buried protons of the protein. Application to the elucidation of protein structure and to the study of dynamical processes is discussed.

Original languageEnglish (US)
Pages (from-to)659-670
Number of pages12
JournalJournal of Molecular Biology
Volume224
Issue number3
DOIs
StatePublished - Apr 5 1992

Keywords

  • TEMPOL
  • e.s.r.
  • n.m.r.
  • protein surface

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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