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What if your mild urea condition unfolds your protein from a globular to a stretched elongated form ? You probably have done CD already to verify that this is not the case.
Jürgen 

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Jürgen Bosch
Johns Hopkins Bloomberg School of Public Health
Department of Biochemistry & Molecular Biology
Johns Hopkins Malaria Research Institute
615 North Wolfe Street, W8708
Baltimore, MD 21205
Phone: +1-410-614-4742
Lab:      +1-410-614-4894
Fax:      +1-410-955-3655
http://lupo.jhsph.edu

On Nov 14, 2012, at 2:57, "Careina Edgooms" <[log in to unmask]> wrote:

Anyone have any advice on how to detect whether my protein is forming oligomers? It is monomeric in the native state but I have reason to believe that it may be oligomerising in mild concentrations of urea (intermediate state).
I have tried cross linking and BN PAGE and they are inconclusive. SE-HPLC does not work because at the concentrations required to produce a signal, this intermediate species aggregates.
I do not have access to an ultracentrifuge. The dynamic light scattering equipment that is available to me is really a poor instrument which will not be sensitive enough to pick up changes in size (we are looking at about 5nm for the monomer and anything from 8nm for the oligomer). The only other option I can think of is SAXS. I will only be able to use that equipment in the middle of next year.
I'm wondering if there is anything else, any other technique or idea that I have not thought about that I could try? I really just would like to show that the stoichiometry of the intermediate species is a multiple of the native state.
If anyone has any suggestions, that would be great.
Thanks
Careina.