title: SEMPRE: spectral editing mediated by paramagnetic relaxation enhancement.
abstract: Paramagnetic relaxation enhancement (PRE) has become a useful and widely applied tool in biomolecular NMR spectroscopy. In particular investigations of large complexes or transient contacts benefit from PRE effects. Frequently such studies involve modification of the biomacromolecules under study. We here present a method for editing NMR spectra by utilizing a soluble gadolinium complex that broadens nuclear spins being at or close to the macromolecule-solvent interface. NOE signals in NOESY spectra are selectively attenuated if surface exposed nuclear spins are involved. HSQC-type spectra with paramagnetic agent contain only signals of the interior of the protein, while the corresponding difference spectra harbor signals allocated to surface spins. Thus, the number of signals can be reduced helping to minimize spectral overlap in large proteins. The method reveals additional information about the localization of spins being helpful for structure determination of large complexes.
authors: Lehrstuhl Biopolymere, Universitat Bayreuth, Bayreuth, Germany.
authors: Ruth
authors: R
authors: Kellner
authors: Christian
authors: C
authors: Mangels
authors: Kristian
authors: K
authors: Schweimer
authors: Stefan J
authors: SJ
authors: Prasch
authors: Philipp R
authors: PR
authors: Weiglmeier
authors: Paul
authors: P
authors: Rösch
authors: Stephan
authors: S
authors: Schwarzinger
mesh_terms: D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D019786:Gadolinium DTPA / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry
chemical_list: D011506:Proteins; D025801:Ubiquitin; D019786:Gadolinium DTPA