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Research was conducted to determine structural characteristics of a two-domain protein fragment of barley lectin using (sup)15N-(sup)1H dipolar coupling method. Results show that the two domains are not rigidly oriented and capable of reorienting independently.

There is a poor correlation between the general order NMR relaxation parameters of the C'-C-alpha vector in the peptide-plane carbonyl and nitrogen nuclei of the protein Escherichia coli flavodoxin. This can be regarded as evidence of local or semilocal anisotropic motion. It is important to measure relaxation parameters of several vectors in a motional unit to describe its dynamic properties. Daragan and Mayo's motional modeling is a good description of the consequences of anisotropic motion in a module that is geometrically linked.

The homonuclear dipolar interaction between adjacent 13C nuclei, otherwise known as the NOE method, is proposed as an alternative to the HCCH-COSY and HCCH-TOCSY techniques of studying large proteins in large magnetic fields. Unlike scalar transfer, magnetization transfer via NOE experiments increases the sensitivity and efficiency of experiments to assign the NMR lines despite the presence of relaxation mechanisms. The difference is approximately less than 20% for proteins with molecular weights of 30 kDa at 17.6 T.