Agitation can cause denaturation of proteins resulting in loss of
activity, precipitation and even cross-beta "amyloid" fibre growth.
Partial unfolding will probably make most proteins more protease sensitive.
Alun.
On 31/03/2011 20:41, gauri misra wrote:
Just an offshoot of the same Questio
I once cleaved a GST tag on the resin using TEV by rocking overnight at 4 C.
I would say it is 100% cutting judging from the gel. One thing to add is
that the protein bound so tight to the beads that cutting tag is the only
way to elute it except by SDS. I haven't had any trouble with TEV and
throm
Just an offshoot of the same Question..
I would like to ask whether the same applies for GST-tag digestion using
thrombin..
No agitation gives better results in the above case too...
Any personal experiences
On Thu, Mar 31, 2011 at 11:29 AM, Klaus Piontek <
klaus.pion...@ocbc.uni-freiburg.de>
