WebinarUsing MDS to observe protein oligomerization
In this webinar we explore protein oligomerization, and look at two case studies where microfluidic diffusional sizing (MDS) was used to observe changing oligomeric states.
Application noteProtein Size as an Indication of Structure
Molecular weight (Mw) is a commonly used, and for many scientists a readily understood, parameter to describe the size of a protein or complex. Here we show how hydrodynamic radius (Rh) can be used in combination with Mw to provide insights into the shape and structure of proteins and illustrate how Mw alone may not always provide a complete picture.
Application noteOligomerization of Interleukin-2
A commercially available human interleukin-2 is assessed by microfluidic diffusional sizing on the Fluidity One across a dilution series. The hydrodynamic radius is observed to increase with increasing concentration, in a way which suggests a monomer-trimer equilibrium with positive cooperativity is established.
PublicationCooperative Assembly of Hsp70 Subdomain Clusters
Wright et al use Microfluidic Diffusional Sizing to probe the oligomerisation of the SBD641 substrate of human Hsp70. The Fluidity One was employed to verify if the fluorescent label used had an affect on measured hydrodynamic radius during the tests.
Application noteDetecting insulin oligomerization using microfluidic diffusional sizing
Insulin monomers self-assemble into hexamers, which is known to affect its level of uptake in the human body. Here we show that Microfluidic Diffusional Sizing (MDS) can be used to detect these changes.