Dear All,
Firstly sorry for asking a non-crystallography
question, but i want help in understanding the data analysis for fitting a
protein-ligand binding data.
Actually i have a protein which is a tetramer in solution and i have done
its flourescence binding with a ligand. I
Dear All
I've been reading several mails that adress the problem of acetylated N-termini
when refining peptide ligands with refmac. I managed to include LINKR records
after running refmacs review restraints as suggested by Eleanor Dodson in one
of the mails I found:
LINKRC ACE I 0
Hi Monica
If protein is Homo-tetramer then one can expect the identical binding
sites. I am also working on homo-dimeric protein which binds to DNA. I
used PRISM to estimate the binding affinity through flourescence
bindingmethod using “SATURATION and NON-LINEAR REGRESSION and ONE SITE
binding
