Protein oligomerization state: Difference between revisions

From NESG Wiki
Jump to navigation Jump to search
mNo edit summary
No edit summary
 
(8 intermediate revisions by 2 users not shown)
Line 1: Line 1:
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.  
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.  


<br>
To make a conclusion about the oligomerization state of a protein one should consider results from several different methods.


It is best to measure the oligomerization state of the protein using many different methods in order to best characterize the system.
The following methods are used within the NESG consortium:


<br>
#[[SDS page gel]]  
 
#[[Gel filtration and light scattering|Gel filtration and static light scattering]][[Gel filtration and light scattering|<br>]]
Within the NESG consortium we&nbsp; the following methods:
#[[NMR determined Rotational correlation time|Rotational correlation time (τ<sub>c</sub>) and NMR relaxation measurement]]
 
#Sedimentation equilibrium
#[SDS page gel]
#Gel filtration  
#Gel filtration with in-line static light scattering  
#Sedimentation equilibrium
#NMR determined rotational correlation time, Tc.

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:

  1. SDS page gel
  2. Gel filtration and static light scattering
  3. Rotational correlation time (τc) and NMR relaxation measurement
  4. Sedimentation equilibrium
Retrieved from "https://nesgwiki.chem.buffalo.edu/index.php?title=Protein_oligomerization_state&oldid=3519"