Table 1 Effect of heavy chain mutations on thermostability in the CH103 lineage

From: Selection of immunoglobulin elbow region mutations impacts interdomain conformational flexibility in HIV-1 broadly neutralizing antibodies

mAb Tm (°C) ΔTm (°C)
UCA 75.6 ± 0.3 --
UCA-P14S 74.63 ± 0.06 −1.0 ± 0.3
UCA-S30G 74.56 ± 0.06 −1.1 ± 0.3
UCA-S30G/S31G 73.8 ± 0.4 −1.8 ± 0.5
I4 64.60 ± 0.01 --
I4-S14P 67.01 ± 0.04 +2.41 ± 0.04
I4-S14P/G30S 68.42 ± 0.02 +3.82 ± 0.03
CH103 65.5 ± 0.1 --
CH103-S14P 66.41 ± 0.03 +0.9 ± 0.1
CH103-S14P/G30S 66.57 ± 0.05 +1.0 ± 0.1
  1. Antibody thermal denaturation profiles were obtained and analyzed by DSC as described in Methods. Data are shown as the mean and standard deviation from a minimum of two replicate measurements. The ΔTm is calculated for each mutant relative to wild-type with error propagated from the standard deviations