title: Automated protein NMR structure determination in solution.
abstract: The main drawback of protein NMR spectroscopy today is still the extensive amount of time required for solving a single structure. The main bottleneck in this respect is the manual evaluation of the experimental spectra. A clear solution to this challenge is the development of automated methods for this purpose. At the current stage of development, this goal has been almost or in a few cases fully reached for favorable cases such as well-behaved, stably folding smaller proteins below the 25 kDa range. For larger and/or more difficult molecules, the input of a human expert is still required. However, even here, automated routines will substantially speed up the structure determination process. In this report, we will summarize recent developments in this field and especially emphasize practical aspects important for a successful automated protein structure determination in solution. An important aspect closely related to structure determination is structure validation. Therefore, we devote a section to automated approaches for this topic.
authors.affiliation: Institute for Biophysics and Physical Biochemistry, University of Regensburg, Regensburg, Germany.
authors.forename: Wolfram
authors.initials: W
authors.lastname: Gronwald
authors.forename: Hans Robert
authors.initials: HR
authors.lastname: Kalbitzer
mesh_terms: D000465:Algorithms; D016477:Artifacts; D001331:Automation; D003198:Computer Simulation; D030562:Databases, Protein; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results; D012996:Solutions; D040681:Structural Homology, Protein
chemical_list: D011506:Proteins; D012996:Solutions