There is a Research coordinator position available immediately at
University of Oklahoma.
*Research Coordinator* *-* *Job Number:* *230192*
*Organization:* Chemistry/Biochemistry
*Job Location:* Oklahoma-Norman-Norman Campus
*Schedule:* Full-time
*Work Schedule:* 8 AM - 5 PM Monday - Friday
There is a NMR manager position available at University of Oklahoma.
*NMR Manager position at University of Oklahoma *
*Organization:* Chemistry/Biochemistry
*Job Location:* Oklahoma-Norman-Norman Campus
*Schedule:* Full-time
*Work Schedule:* Monday - Friday 8-5
*Salary Range:* Target Sa
On behalf of Dr. John Peters, OU
The Peters lab at OU is looking for a postdoctoral associate with a strong
background in metalloproteins.
*Desired qualifications (one or more): *
1) Experience with the expression and purification of oxygen-sensitive
proteins and enzymes
2) Knowledge of crystal
On behalf of Dr. John Peters, OU
The Peters lab at OU is looking for a postdoctoral associate with a strong
background in metalloproteins.
*Desired qualifications (one or more): *
1) Experience with the expression and purification of oxygen-sensitive
proteins and enzymes
2) Knowledge of crystal
Dear all,
Sorry for the off topic.
Looking for suggestions on beamlines for XAFS on proteins with [4Fe-4S]
clusters:
I have two options, one at BNL and another at APS@ANL.
At BNL, I think 6-BM (BMM) seems to be more for biological samples on
metalloproteins on the other hand, ANL has
Hi Anamika,
As far as I understood, the biotin in the elution
buffer is helping your protein to get stripped off from the Avidin column.
So, maybe you dialyze your purified protein (or run FPLC) and get rid of
biotin completely, before you load the protein on to strptavidin coa
. Yet so far, I have not found any example with
different oligomeric states for the *in vivo* assembled (as-purified)
protein VS the *in vitro* reconstituted one.
Regards,
Bhanu
On Mon, Mar 19, 2018 at 11:56 PM, Ethan A Merritt
wrote:
> On Monday, March 19, 2018 2:20:50 PM PDT PULSARSTR
-6383 (phone)
> (214) 645-6353 (fax)
>
> On Mar 19, 2018, at 3:07 PM, PULSARSTRIAN
> wrote:
>
> Dear all,
>
> Sorry for the slightly off-topic question.
>
>I am working on a non-native, *de novo* [4Fe-4S]
> protein, designed as a four-helix
Dear all,
Sorry for the slightly off-topic question.
I am working on a non-native, *de novo* [4Fe-4S]
protein, designed as a four-helix bundle. The *in vitro* reconstituted
protein assembles with [4Fe-4S] (confirmed by EPR) and exists in
monomer-dimer configurat
Dear Dr. Anastassis,
In my practical experience, (homo)
oligomeric helical proteins have greater 222 nm (more negative mdeg) dips
compared to 208 nm, whereas in contrast the coiled coils have greater 208
nm dips over 222, and the depth at 208 nm increases with
Hi Shubhangi,
As Edward suggested, you can try with N-terminal
His tag. For this you can either clone in N-terminal His tagged based
vectors or by site directed insertion of 18 nucleotides coding for 6 His at
the N-terminus region.
But, before that, I suggest
Dear Eike,
You can refer to this article.
The molecular basis of polysaccharide cleavage by lytic polysaccharide
monooxygenases (2016 Feb) by Kristian, Glyn et al. Refer to the
Supplementary Material of the paper for the information of soaking.
(reference PDB id 5ACI).
https:
Hello Every one,
I am trying to purify a human protein in a
bacterial expression system of around 82 kDa (with a 5 kDa His tag, so
fusion protein is 87 kDa) which was cloned in pRSET-A vector. The Problem
is I am not able to get rid of the infamous contamination proteins of
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