Abstract
In the last decade NMR spectroscopy has become an important alternative to X-ray crystallography. The principal advantage of NMR is that it allows the study of biomolecules in solution, thus closer to their real physiological environment. The method is limited, however, to biomolecules of relatively small size due to limitations in spectral resolution and line broadening effects. The upper limit is presently situated around molecular weights of 30 kD. Knowledge of three-dimensional structures might lead, for example, to a better understanding of structure-function relationships or recognition processes. For this purpose, accurate structures are required and, as we shall see, the use of so-called relaxation matrix approaches provides a means to improve the accuracy of the method.
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Kaptein, R., Bonvin, A.M.J.J., Boelens, R. (1997). Biomolecular Structure and Dynamics: Recent Experimental and Theoretical Advances. In: Vergoten, G., Theophanides, T. (eds) Biomolecular Structure and Dynamics. NATO ASI Series, vol 342. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5484-0_9
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DOI: https://doi.org/10.1007/978-94-011-5484-0_9
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