Dear Qiangmin,
may be cleavage site is buried and not accessible for the protease? I am
not familiar with membrane proteins but you can consider this version.
Another question: is your protein N- or C- tagged?
08.04.2013 21:22, Qiangmin Zhang пишет:
> Hello everybody,
>
> I just purified a membra
Hello Qiangmin,
Many membrane proteins like to aggregate in detergent, which
will prevent efficient site specific proteolysis. If you have not
already done so, I suggest running a size exclusion column first to
verify that your protein is monodisperse in your detergent and buffer
of choice.
Hello everybody,
I just purified a membrane protein tagged with GFP, which has a cleavage site
of precession protease. And I got a problem with removing the GFP tag by
precession protease (1mM DTT and 1 mM EDTA were included in the buffer). It can
not cut my protein. I have already tried to dige
Hello everybody,
I just purified a membrane protein tagged with GFP, which has a cleavage site
of preccission protease. And I got a problem with removing the GFP tag by
preccission protease (1mM DTT and 1 mM EDTA were included in the buffer). It
can not cut my protein. I have already tried to di
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1) At least four to get the H-bonding..
2) No - depends on the number and arrangement of beta sheets. Protein
structures vary a great deal!
You could find the % of residues in protein structures which form helices
and beta sheets I guess but there is such huge variation that it may not be
very use
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Dear Friends,I have to ask very basic question. Please provide answer with some
references.1. Whats are the values for maximum and minimum numbers of residues
present in one alpha helix and beta strand?2. Is any fixed (or with some range)
for the percent of beta turns present in protein structur
