What nanoDSF shows about your
monoclonal antibodies
nanoDSF uses your protein's intrinsic fluorescence –
its tryptophan and tyrosine residues – to follow its
unfolding as it denatures in response to an increase in
temperature.
The T
m
is the temperature at which half the protein is
folded, and half is unfolded. For large, multi-domain
proteins such as mAbs, there are multiple T
m
s, which
correspond to the unfolding of different domains. These
are identifiable with high-resolution thermal unfolding
data collected with nanoDSF.
With its high data quality, nanoDSF unveils subtle
changes in T
m
s, multiple domain transitions, and even
reveals the onset of unfolding, T
on
, which pinpoints where
a protein begins unfolding. Low T
on
s indicate a protein is
less stable, even if the T
m
is a relatively high temperature.
