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  • Title: Motional effects on NMR structural data. Comparison of spinach and Escherichia coli acyl carrier proteins.
    Author: Kim Y, Ohlrogge JB, Prestegard JH.
    Journal: Biochem Pharmacol; 1990 Jul 01; 40(1):7-13. PubMed ID: 2196884.
    Abstract:
    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.
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