NMR Spectroscopy for studying interactions of bioactive molecules (CROSBI ID 45179)
Prilog u knjizi | izvorni znanstveni rad
Podaci o odgovornosti
Novak, Predrag ; Jednačak, Tomislav
engleski
NMR Spectroscopy for studying interactions of bioactive molecules
One of the main prerequisites for a successful design of bioactive molecules and drugs is elucidation of three-dimensional structure of small molecular ligands, receptors and their complexes. Key steps in this process involve identification of structural elements and groups responsible for bioactivity. On the other hand, our ability to design novel drug candidates simply from high-resolution structures of biomolecules is still limited. A deeper understanding of molecular mechanisms and dynamics involved in the interaction of ligands with macromolecules is of crucial importance. There are many techniques for probing ligand-receptor interactions such as equilibrium dialysis, fluorescence spectroscopy, capillary electrophoresis, ultrafiltration, etc. Generally, these techniques require time-consuming separation step which might influence binding equilibria or analyte derivatization step which may change ligand activity. NMR spectroscopy is very useful method for characterization of ligand- receptor interactions since it can provide a wealth of information without destroying the sample. In this review a description of the main NMR techniques to study interactions of bioactive molecules with their biological receptors is given and their principal advantages and disadvantages are discussed.
NMR techniques , drug discovery, macrolides, ribosomes, epitopes, drug design
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Podaci o prilogu
1-62.
objavljeno
Podaci o knjizi
Physico-Chemical methods in Drug discovery
Mandić, Zoran
Zagreb: International Association of Physical Chemists (IAPC)
2011.
978-953-56942-0-5