title: Automated analysis of NMR assignments and structures for proteins.
abstract: Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.
authors.affiliation: Center for Advanced Biotechnology and Medicine Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey, 08854-5638, USA. hunter@cabm.rutgers.edu
authors.forename: H N
authors.initials: HN
authors.lastname: Moseley
authors.forename: G T
authors.initials: GT
authors.lastname: Montelione
mesh_terms: D001331:Automation / Q000379:methods; D016222:Fibroblast Growth Factor 2 / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins; D016222:Fibroblast Growth Factor 2