Dear CCP4 colleagues,
We have a protein that is composed of two domains
connected by a short peptide linker. We have some indirect evidence showing
that the two domains may somehow move against each other when exposed to
different pH. It is unlikely to have any obvious secondary structure change
since
each domain behaves like a rigid body. I am wondering whether there is any
“easy”
way, biochemically or biophysically, to monitor the conformational changes in
solution. Many thanks.
As far as I know most of the pH sensing stories are
linked to histidine residue. Can you point me to any references that show a
different pH sensing mechanism (other than His)? Thanks.
Best,
Daniel
