Fig. 1 | Nature Communications

Fig. 1

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

Fig. 1

Thermal destabilization in bnAb affinity maturation. a Representative CD fraction folded derivative plots indicating the observed melting temperature (Tm) for CH103 and its corresponding UCA. b Representative DSC model sum denaturation profiles for both CH103 and its corresponding UCA demonstrating destabilization of the Fab domain (largest amplitude peak) that is consistent with the CD analysis. The onset of Ab denaturation remains the same (~60 °C) for both the germline and mature Abs. c Thermal denaturation of affinity-matured HIV-1 bnAbs (open circle) and their corresponding germline or germline-proximal mAbs (closed circle) was performed by circular dichroism (CD) and/or differential scanning calorimetry (DSC) for Ab pairs of indicated epitope specificity. Data are plotted as the mean and standard deviation from a minimum of two replicate measurements. Error bars are smaller than the data markers at this scale. Data shown for CH01, PG9, and CH31 Ab pairs are the result of single measurements by CD with replicate measurements by DSC reported in Supplementary Table 1

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