Dear Natesh,
as Petri pointed out this is a common behavior for proteins/protein
complexes that deviate substantially from a "globular" shape. It is very
typical for elongated proteins/protein complexes containing e.g. extended
coiled-coil regions. These samples will elute much earlier from a SEC
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
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
What do you mean by mass from SEC? SEC is not a mass determination method
Sent from my iPhone
On 27 Aug 2019, at 06:57, Natesh Ramanathan
mailto:nat...@iisertvm.ac.in>> wrote:
Dear Friends,
Can you share your experience with examples of MALS giving lower
molecular weight (Eg.
Signalling and Structural Biology Lab
The Francis Crick Institute
London, UK
==
about.me/david_briggs
From: CCP4 bulletin board on behalf of Natesh
Ramanathan
Sent: Tuesday, August 27, 2019 6:57:18 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] SEC and MALS
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
