title: Three-dimensional NMR spectroscopy of a protein in solution.
abstract: The geometric information used to solve three-dimensional (3D) structures of proteins by NMR spectroscopy resides in short (less than 5 A) interproton-distance data. To obtain these distances, the 1H-NMR spectrum must first be assigned using correlation and nuclear Overhauser effect (NOE) experiments to demonstrate through-bond (scalar) and through-space connectivities, respectively. Because the NOE is proportional to r-6, distance information can then be derived. The increased resolution afforded by extending NMR experiments into a second dimension enables one to detect and interpret effects that would not be possible in one dimension owing to extensive spectral overlap and much reduced information. A number of small protein structures have previously been solved in this way. Extending this methodology to larger proteins, however, requires yet an additional improvement in resolution as overlap of cross-peaks in the two-dimensional (2D) NMR spectra present a major barrier to their unambiguous identification. One way of increasing the resolution is to extend the 2D-NMR experiments into a third dimension. We report here the applicability of three-dimensional NMR to macromolecules using the 46-residue protein alpha 1-purothionin as an example.
authors.affiliation: Max-Planck Institut für Biochemie, Martinsried bei München, FRG.
authors.forename: H
authors.initials: H
authors.lastname: Oschkinat
authors.forename: C
authors.initials: C
authors.lastname: Griesinger
authors.forename: P J
authors.initials: PJ
authors.lastname: Kraulis
authors.forename: O W
authors.initials: OW
authors.lastname: Sørensen
authors.forename: R R
authors.initials: RR
authors.lastname: Ernst
authors.forename: A M
authors.initials: AM
authors.lastname: Gronenborn
authors.forename: G M
authors.initials: GM
authors.lastname: Clore
mesh_terms: D023181:Antimicrobial Cationic Peptides; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010940:Plant Proteins; D011487:Protein Conformation; D012984:Software
chemical_list: D023181:Antimicrobial Cationic Peptides; D010940:Plant Proteins; C016085:purothionin