Hi Jacob

Not the easiest task... Based on past experience your major issue will be
the incredible abundance of sodium ions in everything.

So assuming you have high quality sodium free solutions and are willing to
work exclusively in plastic, quartz or fused silica - here are a few
thoughts:

1. Na-22 isotope binding. An oldie but goodie.
2. Sodium-reactive dye equilibrium (see e.g. reference I put at the end)
3. Flame or ion coupled plasma spectroscopy. Very nice to do given the
marvellous sodium band.
4. Sodium selective glass electrode (requires more solution of your analyte
than the other methods)

Overall the key component to these methods is your ability to displace the
sodium with something else prior to measuring the effect of titration the
ion back. Isotopic Na is easier in this regard - but at a cost...

Hope this helps.

Artem

https://bmcresnotes.biomedcentral.com/articles/10.1186/1756-0500-6-556

https://www.google.com/url?sa=t&source=web&rct=j&url=http://clinchem.aaccjnls.org/content/clinchem/24/4/580.full.pdf&ved=2ahUKEwis5KL_vM_lAhXCmuAKHY2cAVQQFjAFegQIARAB&usg=AOvVaw0Yhz23Yr_ulB85MDQspIFl&cshid=1572833723049


On Sun, Nov 3, 2019, 20:41 Keller, Jacob <[email protected]> wrote:

> Dear Crystallographers,
>
>
>
> Does anyone know of a good biophysical way to identify or quantify sodium
> ion binding to a protein, besides crystallography and ITC? Is this possible
> with SPR, perhaps? Mass spec? Gel shifts? Examples would be greatly
> appreciated!
>
>
>
> All the best,
>
>
>
> Jacob Keller
>
>
>
>
>
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> Jacob Pearson Keller
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>
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