Sequence-Specific Assignment of Aromatic Resonances of Uniformly ~(13)C,~(15)N-Labeled Proteins by Using ~(13)C- and ~(15)N-Edited NOESY Spectra

摘要

The precision of a protein structure determined by NMR spectroscopy is strongly influenced by the number of long-range NOE interactions per residue. Aromatic and methyl-containing residues are frequently located in the hydrophobic interior of proteins and yield long-range NOE interactions. Methyl groups have become the major focus in the structure determination of large proteins in recent years.On the other hand, aromatic groups have not received equal attention because their sequence-specific assignment is extremely difficult, especially for proteins larger than 25 kDa.