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Techniques in few words

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Nuclear Magnetic Resonance (NMR) is a spectroscopic technique allowing the study of matter at the atomic level. In particular, it is possible to establish the three-dimensional structure and study the dynamics of biological macromolecules such as peptides, proteins and nucleic acids. One of the major advantages of NMR is that the molecules are studied in solution under conditions close to physiological conditions.

The knowledge of the 3D structure of biomolecules is essential but not sufficient to understand their biological role. The elucidation of their interactions with various partners is essential to understand the biological mechanisms which govern life.

Molecular modelling techniques are used to build the 3D structures of molecules from the NMR data. Alternatively, in the absence of experimental data, homology modelling techniques (also known as comparative modelling) are used to build 3D structures. This class of methods utilizes the 3D structures of proteins showing sequence similarities to a target protein of unknown structure to build an atomic-resolution model of this target.

Docking techniques allow to build molecular models of complexes using experimental data resulting from NMR or other techniques (mutagenesis, …).

The internal dynamics of molecules is also studied by NMR in order to characterize the motions of the various parts of a molecule, either isolated or in complex with other molecules.