Hi,
Thank you for all replies.
Sincerely
Debajyoti
On Mon, 25 Aug 2008 Artem Evdokimov wrote :
>If your protein precipitates at low ionic strength you may want to establish
>what concentration of salt does it tolerate (by slowly diluting a fraction
>of your pool with water just until you s
You can try TOPS.
http://www.tops.leeds.ac.uk/
Best,
Nian
On Fri, Aug 22, 2008 at 8:57 AM, Buz Barstow <[EMAIL PROTECTED]> wrote:
> Dear All,
>
> Does anyone know of a program that is capable of drawing the secondary
> structure of a protein molecule?
>
> I'd really like to be able to take a prot
Phil
Squaring the (i.e. the best estimate of Ftrue) that Truncate
estimates does not give you (the best estimate of Itrue):
= Integral[0:infinity] sqrt(J) p(J|I) dJ
var(F) = Integral[0:infinity] (sqrt(J)-)^2 p(J|I) dJ
= Integral[0:infinity] J p(J|I) dJ
Also, for very large proteins you should not boil the samples - if you must
heat, just go to 50-60C for a few minutes. You also may have better luck
with CTAB-PAGE rather than SDS-PAGE (CTAB tends to smear less, for some
reason).
Artem
-Original Message-
From: CCP4 bulletin board [mailto:
If your protein precipitates at low ionic strength you may want to establish
what concentration of salt does it tolerate (by slowly diluting a fraction
of your pool with water just until you see precipitation) then try to adjust
your cation exchange conditions so that you load with enough salt to k
You're right. The smoothed is used for the Truncate procedure,
though it is difficult in the very low resolution bins. Also it
doesn't allow for pseudo-translations, which it should.
As you say, the linear fit is only used to put data on a very rough
absolute scale. This isn't necessary, b
Phil
OK I admit I didn't delve very deeply into the code, but looking at the
printer output it obviously does do a linear fit to the Wilson plot to
get an overall B & scale. However, looking at the man page (if all else
fails read the documentation!) I see that it does say that this is only
used
Sorry for the off-topic question. I am trying to separate by SDS-PAGE
really big proteins (>500 kDa), and lower percentage (3-8%) acrylamide
gels do not do the trick. Based on literature searches, acrylamide-agarose
composite gels seem the way to go. Is anyone willing to share a protocol?
I can
Hello everyone:
Sorry for the off-topic question. I am trying to separate by SDS-PAGE really
big proteins (>500 kDa), and lower percentage (3-8%) acrylamide gels do not do
the trick. Based on literature searches, acrylamide-agarose composite gels seem
the way to go. Is anyone willing to share a
Hi again,
Thank you for all you have replied. I suspect the sonnication for such a bad
result. I am just wondering if I can use Histidine instead of Imidazole and
then buffer exchange to go for Cation exchanger.
Does Imidazole had any bad effect in protein. I have experienced that the
protei
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