Motional effects on NMR structural data. Comparison of spinach and Escherichia coli acyl carrier proteins.
Proteins in solution need not exist in a single rigid structure but can exist in a dynamic equilibrium among structural forms. The problems that this poses for structure determination using nuclear Overhauser effect data from two-dimensional NMR experiments are discussed and illustrated with data on functionally equivalent proteins from two different species. One of these proteins, acyl carrier protein from Escherichia coli, shows a single set of resonances, easily interpreted on the basis of a single rigid structure. However, the related protein, acyl carrier protein from spinach, shows two sets of resonances, suggesting that two conformers in dynamic equilibrium would be a better structural model.
Chemistry Department, Yale University, New Haven, CT 06511.
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Y
Kim
J B
JB
Ohlrogge
J H
JH
Prestegard
D000213:Acyl Carrier Protein; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013696:Temperature; D014675:Vegetables / Q000032:analysis
D000213:Acyl Carrier Protein