title: Proton Transverse Relaxation as a Sensitive Probe for Structure Determination in Solid Proteins.
abstract: Solid-state nuclear magnetic resonance (NMR) spectroscopy has been successfully applied to elucidate the atomic-resolution structures of insoluble proteins. The major bottleneck is the difficulty to obtain valuable long-distance structural information. Here, we propose the use of distance restraints as long as 32 Å, obtained from the quantification of transverse proton relaxation induced by a methanethiosulfonate spin label (MTSL). Combined with dipolar proton-proton distance restraints, this method allows us to obtain protein structures with excellent precision from single spin-labeled 1 mg protein samples using fast magic angle spinning.
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Petra
authors.initials: P
authors.lastname: Rovó
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Kristof
authors.initials: K
authors.lastname: Grohe
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Karin
authors.initials: K
authors.lastname: Giller
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. rali@nmr.mpibpc.mpg.de.
authors.forename: Rasmus
authors.initials: R
authors.lastname: Linser
mesh_terms: D057230:Limit of Detection; D009682:Magnetic Resonance Spectroscopy; D015335:Molecular Probes; D011506:Proteins / Q000737:chemistry*; D011522:Protons
chemical_list: D015335:Molecular Probes; D011506:Proteins; D011522:Protons
keywords: nuclear magnetic resonance; paramagnetic relaxation enhancement; proteins; spectroscopy; structure determination