The structural characterization of multidomain protein complexes was studied using spin-relaxation and dipolar coupling measurements. The internuclear anisotropy of molecular tumbling was determined by NMR approaches. It was found that the interdomain interface was formed by hydrophobic patches. The interdomain dynamics allowed the L8, 144, and V70 groups to interact with other molecules. The features of anisotropic tumbling and tensor determination were explored by using computer-generated relaxation data.
Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements
ASSFALG, Michael;
2004-01-01
Abstract
The structural characterization of multidomain protein complexes was studied using spin-relaxation and dipolar coupling measurements. The internuclear anisotropy of molecular tumbling was determined by NMR approaches. It was found that the interdomain interface was formed by hydrophobic patches. The interdomain dynamics allowed the L8, 144, and V70 groups to interact with other molecules. The features of anisotropic tumbling and tensor determination were explored by using computer-generated relaxation data.
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