Biological molecule structural characterization

In biopharmaceutics, effective methods are strongly needed, not only to characterize the interactions of drugs and vehicles with biological structures in order to optimize pharmaceutical vehicle systems, but also to study the interactions between biological molecules and to investigate immunoreactions. 

Biological studies in combination with powerful analytical tools, especially modern MS, for the structural characterization of low-abundance complex molecules, has enabled the phenotyping of numerous examples of these structures. 

The development of HR-MAS probes has resulted in several technical developments extending beyond the analysis of SPS products. HR-MAS NMR has also been used for structure determination of very small samples containing submicrogram quantities of biological molecules 35 it has been used for the biochemical characterization of tissue samples in normal and disease states 36 and more recently it has been used in a screening role to identify substances with binding activity from a mixture of compounds,37 as described later in this review. 

It is clear from the discussion of metal homeostasis that the fuU characterization of a protein requires not only its study in the isolated form but also the investigation of its relevant interactions. Therefore, the interactions of metal-binding proteins with small molecules and other proteins are an obvious perspective in biological inorganic research. This implies the importance of the identification and structure characterization of weak protein-protein complexes that represent the key steps of the biochemical processes discussed here. Moreover, metal-mediated protein-protein interactions are just beginning to be identified and will become an important field of research. 

---