Abstract

NMR spectroscopy is the only technique capable of determining the three-dimensional structures of macromolecules in solution at atomic resolution [1,2]. The explosive growth in the field of NMR spectroscopy originated with the development of pulsed Fourier transform NMR spectroscopy by Ernst and Anderson [3] and the conception of multidimensional NMR spectroscopy by Jeener [4]. The complexity of NMR spectra of proteins can be overcome thanks to the fact that they are built from a limited number of common blocks, the aminoacids, whose fingerprint are easily recognizable [5]. Standard strategies have been developed to obtain resonance assignments, and, from the latter, a number of dipolar constraints (NOE) high enough to allow solution structure determination [5].

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