title: A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments.
abstract: The determination of the three-dimensional structure of a protein or the study of protein-ligand interactions requires the assignment of all relevant nuclei as an initial step. This is nowadays almost exclusively performed using triple-resonance experiments. The conventional strategy utilizes one or more pairs of three dimensional spectra to obtain redundant information and thus reliable assignments. Here, a modified strategy for obtaining sequence specific assignments based on two dimensional amino acid type selective triple-resonance experiments is proposed. These experiments can be recorded with good resolution in a relatively short time. They provide very specific and redundant information, in particular on sequential connectivities, that drastically increases the ease and reliability of the assignment procedure, done either manually or in an automated fashion. The new strategy is demonstrated with the protein domain PB1 from yeast CDC24p.
authors.affiliation: Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Str. 10, D-13125, Berlin, Germany.
authors.forename: Mario
authors.initials: M
authors.lastname: Schubert
authors.forename: Dirk
authors.initials: D
authors.lastname: Labudde
authors.forename: Dietmar
authors.initials: D
authors.lastname: Leitner
authors.forename: Hartmut
authors.initials: H
authors.lastname: Oschkinat
authors.forename: Peter
authors.initials: P
authors.lastname: Schmieder
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D011506:Proteins