title: Automated analysis of nuclear magnetic resonance assignments for proteins.
abstract: Recent developments in protein NMR technology provide spectral data that are highly amendable to analysis by computer software systems. Automated methods of analysis use constraint satisfaction, pseudoenergy minimization, directed search, neural net, simulated annealing, and/or genetic algorithms to establish sequential links and sequence-specific assignments. The most advanced systems provide automated analysis of complete backbone and extensive side-chain resonance assignments for proteins of 50-150 amino acids.
authors.affiliation: Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, NJ 08854-5638, USA.
authors.forename: D E
authors.initials: DE
authors.lastname: Zimmerman
authors.forename: G T
authors.initials: GT
authors.lastname: Montelione
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008968:Molecular Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012984:Software
chemical_list: D000596:Amino Acids; D011506:Proteins