Protein oligomerization state: Difference between revisions
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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: | |||
#[[SDS page gel]] | #[[SDS page gel]] | ||
#[[Gel filtration and light scattering|Gel filtration]] | #[[Gel filtration and light scattering|Gel filtration]] | ||
#[[Gel filtration and light scattering| | #[[Gel filtration and light scattering|Static light scattering]] | ||
#[[NMR determined Rotational correlation time|Rotational correlation time (τ<sub>c</sub>) and NMR relaxation measurement]] | |||
#[[NMR determined Rotational correlation time]] | #Sedimentation equilibrium | ||
Revision as of 21:50, 16 December 2009
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:
- SDS page gel
- Gel filtration
- Static light scattering
- Rotational correlation time (τc) and NMR relaxation measurement
- Sedimentation equilibrium