Hi Todd,
Do you mean reversible or irreversible dimers?
If the binding is reversible, then once crystal growth starts, Le
Chatelier's principle should take over, pull the equilibrium toward
monomer, and you should see minimal impact of dimer on your monomer
crystals. The same would be true in
Dear all,
If I may add that I find the statement
First, remember that gel filtration elution volumes are independent
of conditions like flow rate and protein concentration (unless there
are nonspecific interactions at high concentration), but like I
described before temp is a factor.
a
Thank you. Now I understand the difference. I thought there was separation.
Maia
Xuewu Zhang wrote:
Hi Maia,
I have seen your post regarding this before and I just want to point
out that you may have confused AUC (analytical ultracentrifugation)
with gradient-based ultra-centrifugation
Hi ccp4bb
Could you please send me some references with the sedimentation
equilibrium calculations of Kd, monomer/dimer ratio etc.
Maia
Maia Cherney wrote:
Thank you. Now I understand the difference. I thought there was
separation.
Maia
Xuewu Zhang wrote:
Hi Maia,
I have seen your post
Hi Maia, this review and website might be a good place to start:
http://analyticalultracentrifugation.com/images/AUCinProteinScience.pdf
http://analyticalultracentrifugation.com/default.htm
Kushol
Kushol Gupta, Ph.D.
Research Associate
Van Duyne Laboratory - HHMI/Univ. of Pennsylvania School
- Original Message -
From: Anastassis Perrakis a.perra...@nki.nl
To: CCP4BB@JISCMAIL.AC.UK
Sent: Wednesday, August 11, 2010 2:10:16 AM GMT -08:00 US/Canada Pacific
Subject: Re: [ccp4bb] monomer-dimer
Dear all,
If I may add that I find the statement
First, remember that gel filtration
Hello Intekhab,
Your results do not seem surprising at all. It is not uncommon for molecular
interactions such as dimerization to be more stable at lower temperatures, and
this is exactly why you are seeing the shift to higher elution volumes at lower
tempratures. At lower temperatures, both
To determine the oligomeric state of a protein (monomer or dimer in your
case), it's useful to use the PISA server. You upload your pdb file from
the crystal structure.The server calculates the areas of interfaces
(buried area) and deltaG (change in Gibbs energy) upon oligomer
dissociation.
Dear Intekhab
Let me just add to this that gel filtration is not an accurate method for
determination of molecular mass, because the migration on the column depends
on the shape of the protein.
The following methods can be used to determine molecular mass irrespective
of shape:
- MALLS
Dear
That was a quite enlightening discussion!!
I am grateful to you guys for your time!!
I will definitily try some of these to get a clear answer.
Regards
Intekhab alam
On Tue, Aug 10, 2010 at 8:38 AM, Bostjan Kobe b.k...@uq.edu.au wrote:
Dear Intekhab
Let me just add to this that gel
Small angle x-ray solution scattering (SAXS) can also give you molecular
weight, though not quite as accurately as the best static light scattering.
While SAXS is preferably done on monodisperse systems extrapolated to infinite
dilution, cases in which the monomer and dimer are in equilibrium
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