Intermolecular and intramolecular interactions are crucial for almost all
processes in chemistry, biology and biochemistry, and one of the most powerful
techniques for monitoring these interactions is NMR spectroscopy. Many NMR
experiments study biomolecules or small organic molecules under non-natural
conditions, but these are still very similar to the native environments. In this chapter,
our aim is to discuss NMR spectroscopy applications to drug design, enzyme
inhibition, and the monitoring of host-guest interactions during the development of
some novel drug formulations. In addition, other important protein-ligand and proteinprotein
interactions will be discussed. Two NMR approaches are conducted for
monitoring these interactions: one of these is based on the isotopic labeling of proteins
and the other is based on the study of small molecules. Both techniques have a high
impact on the examined cases. Finally, intermolecular and intramolecular interactions
are used to study different metabolic pathways, and one very important NMR
spectroscopy application includes metabolomics, where elucidation of characteristic
chemical fingerprints for various biochemical processes can be achieved; this technique
can be used to compare symptomatic, infected and healthy subjects.
Keywords: CSP, DOSY, HSQC, Molecular interactions, NMR screening,
NOESY, Protein-based NMR, Relaxation, ROESY, Small-molecule-based NMR,
STD and metabolomics.
