You're being way too generic. There are some rules of thumb but they're
vague.
1) common proteins do not like extreme pH. Below 5 and above 8 are extreme,
as far as I am concerned.
2) proteins do not like to be near or pass through their pI. If you must -
do it quickly, at high dilution.
3) never use 100% of your protein in one fell swoop- if you have to dialyze
against a previously unexplored condition save some of your stuff in case
the condition sucks.
You can check for aggregation using light scattering and other techniques.
You can check for proper folding using CD and proton-NMR. Good luck.
A.G.E.
<bgkrishnan at hotmail.com> wrote in message
news:20021010190916.24382.qmail at ww02.hostica.com...
> Hi,
> Is there any method /resource to judge if a protein is stable at a given
pH? In other words how
> does one know if a particular protein at 4 Degree C is stable and folds
correctly in a buffer of
> certain pH?
> thanks,
>>http://biowww.net/mynews/tree.php?group_name=bionet_molbio_proteins&begin=0
