Application of NMR in structural proteomics: screening for proteins amenable to structural analysis.
In the time of structural proteomics when protein structures are targeted on a genome-wide scale, the detection of "well-behaved" proteins that would yield good quality NMR spectra or X-ray images is the key to high-throughput structure determination. Already, simple one-dimensional proton NMR spectra provide enough information for assessing the folding properties of proteins. Heteronuclear two-dimensional spectra are routinely used for screenings that reveal structural, as well as binding, properties of proteins. NMR can thus provide important information for optimizing conditions for protein constructs that are amenable to structural studies.
Rehm
Till
T
Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152 München, Germany.
Huber
Robert
R
Holak
Tad A
TA
D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics
D011506:Proteins