Protein oligomerization state: Difference between revisions
Jump to navigation
Jump to search
mNo edit summary |
mNo edit summary |
||
| Line 10: | Line 10: | ||
#[[SDS page gel]] | #[[SDS page gel]] | ||
#[[Gel filtration and light scattering|Gel filtration]] | #[[Gel filtration and light scattering|Gel filtration]] | ||
#Gel filtration with in-line static light scattering | #[[Gel filtration and light scattering|Gel filtration with in-line static light scattering]] | ||
#Sedimentation equilibrium | #[[Sedimentation equilibrium]] | ||
#NMR determined rotational correlation time, Tc. | #NMR determined rotational correlation time, Tc. | ||
Revision as of 17:33, 16 November 2009
Determinations of a proteins oligomeric state in an NMR sample can sometimes be a challenge. This is especially true in the case of oligomeric mixtures, such as specific or non-specific aggregation.
It is best to measure the oligomerization state of the protein using many different methods in order to best characterize the system.
Within the NESG consortium we the following methods:
- SDS page gel
- Gel filtration
- Gel filtration with in-line static light scattering
- Sedimentation equilibrium
- NMR determined rotational correlation time, Tc.