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 Lesk, Henriette Molinari, Andrea Motta, Neri Niccolai, Annalisa Pastore

Research output: Contribution to journalArticle

52 Citations (Scopus)

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

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Magnetic Resonance Spectroscopy
Protons
Proteins
Spin Labels
Egg White
Protein Conformation
Protein Folding
Free Radicals

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

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title = "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",
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.",
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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. / Esposito, Gennaro; Lesk, Arthur; Molinari, Henriette; Motta, Andrea; Niccolai, Neri; Pastore, Annalisa.

In: Journal of Molecular Biology, Vol. 224, No. 3, 05.04.1992, p. 659-670.

Research output: Contribution to journalArticle

TY - JOUR

T1 - 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

AU - Esposito, Gennaro

AU - Lesk, Arthur

AU - Molinari, Henriette

AU - Motta, Andrea

AU - Niccolai, Neri

AU - Pastore, Annalisa

PY - 1992/4/5

Y1 - 1992/4/5

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