In the past several years a significant number of new multidimensional NMR methods have been developed to study molecular dynamics spanning a wide range of time scales. Applications involving a large number of biological systems have emerged and correlations with function established. Unique insights are obtained that are not available from structure alone, indicating the importance of dynamics studies for understanding function.
In combination with magic angle spinning, dipolar recoupling yields solid state NMR spectral assignments and provides constraints on internuclear distances and torsion angles. The method offers a fresh approach to structural studies of a variety of systems that cannot be examined with conventional tools available to structural biology.
Structure determination of biomolecules by NMR has traditionally been based on nuclear Overhauser effects (NOEs). Now there are additional sources of information that can complement NOEs in cases where positioning of remote parts of molecules is important, and where extension to larger and more complex systems is desired.
NMR spectroscopy is one of the principal experimental techniques of structural biology, with abilities to determine atomic resolution structures as well as investigate dynamics and intermolecular interactions of biological macromolecules. There is plenty of room for continued progress of this young branch of science, based on further technical advances as well as innovative funding strategies and project organization.
NMR studies of domains, dissected from large modular proteins, are described. Particular emphasis is placed on modules from the extracellular proteins fibrillin-1 and fibronectin.
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