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Studying Conformational Changes Which Occur when Proteins Bind Metal Ions

In this webinar the use of the surface characterization technique Dual Polarization Interferometry (DPI) to study the structural changes that proteins undergo when they bind metal ions will be discussed. Metal ions play a role in a wide range of everyday biological processes involving proteins. It is important to understand their mechanism of action as diseased states, including prion ('mad cow') diseases, result in changes in protein - metal ion binding behaviors. Metal ions are known to modulate the activity of proteins through a number of mechanisms including: Acting as an intermediate in protein:ligand and protein:protein interactions;Bridging amino acid residues and domains (often associated with 'putative' structural changes); Playing a direct role in active site exchanges, acting either in an electron transfer role or as a nucleophilic catalyst; Although there are a wide range of metal ions available, biological processes are very often metal ion specific. Therefore understanding not just which metal ions bind but also the structural consequences of binding, offers important mechanistic insights into their mode of action.The conformational changes effected in proteins by metal ion binding can be extraordinarily large. The webinar will include a brief overview of DPI. Differences in the practical approach when compared to other optical techniques will be examined. A number of examples of metal ion binding of relevance to a diverse range of biological processes from the blood clotting cascade to infectious diseases such as prion diseases will be discussed.

Type:	Dual Polarization Interferometry (DPI)
Duration:	27 minutes
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