Table 2 TRAF3IP1 N-terminal mutations result in lower stability of the IFT54/IFT20 complex.

From: Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in microtubule stabilization

Sample

Secondary structure determination

Thermal unfolding

 

α (%)

β (%)

Turn (%)

Unstructured (%)

Melting temperature TM (°C, ± s.d.)

CrIFT54-WT/CrIFT20

46

9

16

29

51.15±0.040

CrIFT54-V126A/CrIFT20

39

11

19

31

48.75±0.061

CrIFT54-V126M/CrIFT20

35

16

18

31

48.15±0.106

CrIFT20

71

1

6

22

41.62±0.146

  1. Secondary structure determination and thermal unfolding using circular dichroism spectroscopy for WT as well as p.V126A and p.V126M mutants of CrIFT54 (corresponding to the human p.V125A and p.V125M mutations) in complex with CrIFT20.
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