Because MALS can capture distinct migrant form of the same protein,
sometimes  protein with disorder and elongated structure behave differently
in  SEC. In SEC we can't distinguish them.  Whereas MALS have scattering at
three different angles,  by that we can captures those multiple forms of
the same protein.
Please provide the image for more information.

On Tue, Aug 27, 2019, 12:30 PM Petri Kursula <[email protected]>
wrote:

> Hi,
> that's typical behaviour for an elongated/disordered molecule, given that
> SEC separates based on hydrodynamic radius, not MW.
> Petri
>
> Petri Kursula
> ----------
> Professor
> ----------
> Department of Biomedicine
> University of Bergen, Norway
> http://www.uib.no/en/rg/petrikursula
> <http://www.uib.no/en/persons/Petri.Kursula>
> [email protected] <[email protected]>
> ----------
> Faculty of Biochemistry and Molecular Medicine
> University of Oulu, Finland
> ----------
>
>
>
>
>
>
> On 27 Aug 2019, at 07:57, Natesh Ramanathan <[email protected]
> <[email protected]>> wrote:
>
> Dear  Friends,
>
>         Can you share your experience with examples of MALS giving lower
> molecular weight (Eg. Monomer) and  SEC giving higher molecular weight (Eg.
> Dimer),  for the same protein sample?
>
>       If you have/know any published paper, can you please point me to
> that reference paper or send me the paper?
>
> Many thanks.
> Best regards,
> Natesh
>
>
> --
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> Assistant Professor,
> School of Biology,
> Indian Institute of Science Education and Research Thiruvananthapuram
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