Ho Jun Lee,
Have you thought about differential scanning fluorimetry (Thermofluor)? With
this biophysical technique you can characterize protein-ligand interactions and
screen a wide variety of ligands using minimal concentration of ligand and
protein. All you need is a quantitative PCR
Feng Lei,
I would personally recommend slowing down the process of nucleation either by
lowering the temperature of crystallization or by utilizing Al's oil. These are
two powerful ways to slow the overall kinetics of crystallization. Here is a
relevant reference for you:
Dear All,
On behalf of Dr. Jia-huai Wang, I post this message. For inquiries please
contact Dr. Wang directly at jw...@red.dfci.harvard.edu
Postdoctoral Position in
Structural Biology of Immune Receptors:
There is an immediate opening for a
postdoctoral position in protein crystallography at
On Thu, 9 Aug 2012 10:05:19 -0400, Dr. Lorenzo Finci
lfi...@hotmail.com wrote:
Danilo,
The protein cavity can be analyzed utilizing the program Voidoo (
Kleywegt GJ, 1994). This program uses an atomic-flattening algorithm
based on a 3-dimensional grid to locate and delineate different
Danilo,
The protein cavity can be analyzed utilizing the program Voidoo ( Kleywegt GJ,
1994). This program uses an atomic-flattening algorithm based on a
3-dimensional grid to locate and delineate different cavities. A Van Der Waals
cavity can further be generated with a probe radius with a
Dear Colleagues,
I have a question for all of you bioinformatics oriented structural biologists:
How do I predict the sites of protein-protein interactions between two
receptors that have been proven to interact biochemically but lack specific
details regarding proximity. This is not a
. Lorenzo Finci wrote:
Anita, In terms of the basics:Thermodynamic stability of a protein is related
to Gibbs Free Energy of unfolding. The Gibbs Free Energy is made of
temperature, enthalpy and entropy (Delta G = Delta H - T Delta S). At Delta G
equivalent to zero, the concentration of folded protein is equivalent
Jan,
I agree that the DTNB assay (Ellman's Reagent) can be used to quantify exposed
Cysteines. Alternatively, you could do site directed mutagenesis and mutate
significant amino acids responsible for the conformational change from the open
to the closed state, with hopes to lock the protein
Petros,
It has indeed been speculated that high concentrations of Magnesium and/or
other metals present in the cell lysate effect the binding of the
Histidine-tag, and thus specific conditions for binding and elution need to be
optimized for specific elution of your target protein. I believe
Etros, It has indeed been speculated that high concentrations of Magnesium
and/or other metals present in the cell lysate effect the binding of the
Histidine-tag, and thus specific conditions for binding and elution need to be
optimized for specific elution of your target protein. I believe
Protein Biochemist Position in Structural Neuroscience
There is an immediate opening for an enthusiastic and experienced protein
biochemist to join the international structural biology laboratory of Jia-Huai
Wang based at Peking University in Beijing, China. The research is focused on
the
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