Protein oligomerization state: Difference between revisions
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#[[SDS page gel]] | #[[SDS page gel]] | ||
#[[Gel filtration and light scattering|Gel filtration]] | #[[Gel filtration and light scattering|Gel filtration and static light scattering]][[Gel filtration and light scattering|<br>]] | ||
#[[NMR determined Rotational correlation time|Rotational correlation time (τ<sub>c</sub>) and NMR relaxation measurement]] | #[[NMR determined Rotational correlation time|Rotational correlation time (τ<sub>c</sub>) and NMR relaxation measurement]] | ||
#Sedimentation equilibrium | #Sedimentation equilibrium | ||
Latest revision as of 16:33, 6 January 2010
In order to correctly interpret NOESY data during structure determination it is necessary to know the oligomerization state of the protein at NMR conditions. This can sometimes be challenging, especially in the case of mixtures of monomers and oligomers, and specific or non-specific aggregation.
To make a conclusion about the oligomerization state of a protein one should consider results from several different methods.
The following methods are used within the NESG consortium: