4
Thermal unfolding experiments
The mAbs were subject to a linear thermal ramp
(1 °C/min, from 25 to 90 °C), and tryptophan
fluorescence at 350 and 330 nm was collected at a
rate of 10 datapoints per minute. Unfolding
transition midpoints were determined automatically
from the 2
nd
derivative of the fluorescence ratio
(F350/F330).
References
Adair JR, Howard PW, Hartley JA, Williams DG,
Chester KA (2012) Antibody-drug conjugates - a
perfect synergy. Expert opinion on biological
therapy 12: 1191-1206
Yang X, Ambrogelly A (2014) Enlarging the
repertoire of therapeutic monoclonal antibodies
platforms: domesticating half molecule exchange to
produce stable IgG4 and IgG1 bispecific antibodies.
Current opinion in biotechnology 30C: 225-229
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