Solution NMR structure determination of proteins revisited.
This 'Perspective' bears on the present state of protein structure determination by NMR in solution. The focus is on a comparison of the infrastructure available for NMR structure determination when compared to protein crystal structure determination by X-ray diffraction. The main conclusion emerges that the unique potential of NMR to generate high resolution data also on dynamics, interactions and conformational equilibria has contributed to a lack of standard procedures for structure determination which would be readily amenable to improved efficiency by automation. To spark renewed discussion on the topic of NMR structure determination of proteins, procedural steps with high potential for improvement are identified.
Billeter
Martin
M
Department of Chemistry, University of Gothenburg, Box 462, 40530, Gothenburg, Sweden. martin.billeter@chem.gu.se
Wagner
Gerhard
G
Wüthrich
Kurt
K
D001669:Biochemical Phenomena; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D011506:Proteins