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Figure 6
(a) UV280 intensity evolution profiles of the SEC-SWAXS of TTR–tafamidis and TTR–tolcapone solutions (R = 10), containing 8 M urea at 37°C. The arrow indicates a broad band that is likely contributed by dissociated TTR fractures in the former case. (b) Corresponding SWAXS profiles over the SEC-SWAXS elution peak. The calculated SWAXS profile of the 4d7b crystal structure of TTR–tafamidis largely overlaps with the SWAXS data, especially in the low-q region. Note that in Fig. 5[link](a) the elution time of the P1 peak assigned to the TTR octamer falls behind the elution peak of the smaller TTR tetramer in (a). The longer elution time is attributed to the unfolded/extended protein conformation in the TTR octamer, as similarly observed previously in the elution of unfolded bovine serum albumin (Yeh et al., 2017BB36) shown in Fig. S7.

Journal logoJOURNAL OF
APPLIED
CRYSTALLOGRAPHY
ISSN: 1600-5767
Volume 58| Part 4| August 2025| Pages 1373-1383
https://doi.org/10.1107/S1600576725004716
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