The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein.

By A. Vermeer, W. Norde. Biophysical Journal, 2000

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Improving the biophysical properties of anti-ricin single-domain antibodies☆ (2015, background): “Unlike traditional antibodies, which normally aggregate and lose their ability to function after being heated above their melting temperature (Tm; the temperature at which half the protein is unfolded) [8], sdAbs are often found to recover their binding ability even after repeated thermal denaturati”
Stability engineering of antibody single-chain Fv fragments. (2001, background): “First, most data are available on scFvs, although it should be mentioned that other recombinant antibody fragments and even whole antibodies have also been studied regarding their stability (e.g. Shimizu et al., 1992; Yasui et al., 1994; Shimba et al., 1995; Vermeer & Norde, 2000).”