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. Author manuscript; available in PMC: 2017 Jul 15.
Published in final edited form as: ACS Chem Biol. 2016 Apr 29;11(7):1852–1861. doi: 10.1021/acschembio.5b01035

Figure 2. Sequences, isoforms and thermal stabilities of Fc variants.

Figure 2

(a) Protein primary sequences of the IgG1 Fc variants around the C’E loop (Gln295-Thr299). Asn297 is shown in bold and underlined and Thr299 is shown in bold. Mutations are shown in red. (b) ESI-MS analysis of the purified Fc variant glycoforms. Relative abundance of glycoforms for each variant is normalized to the most abundant glycoform observed, and only those glycoforms that have relative abundance above 0.15 are shown. G# refers to the number of Gal on the two arms and F to fucosylation of the initial GlcNAc residue. (c–f) DSC analysis of the stability of Fc variants WT, FY, QA and FA. The baseline-adjusted DSC trace (black line) showed a two-peak feature for each variant which could be deconvoluted (grey lines) to the melting of CH2 (lower temperature, Tm1) and CH3 (higher temperature, Tm2) domains. The protein primary sequence of the C’E loop and Tm1 for each variant are shown above the DSC curves.