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. Author manuscript; available in PMC: 2013 Oct 1.
Published in final edited form as: Curr Opin Cell Biol. 2012 Jul 6;24(5):620–627. doi: 10.1016/j.ceb.2012.05.014

Table 1.

Homo-dimerization affinities from AUC measurements at 25°C

Protein Description KA (x 104) M−1 Ref.
Xenopus C-cadherin EC1–5
WT Wild Type 1.56 [48]
Mouse E-cadherin EC1–2
WT Wild Type (human) 1.25 [49]
WT Wild Type 1.04 [4]
WT Wild Type 1.01 [16]
W2A Strand-swap mutant 0.11
Ala-Ala N-terminal extension Strand-swap mutant 0.12
E89A Strand-swap mutant 0.34
Asp-Trp deletion at N-terminus Strand-swap mutant 0.15
K14E X-dimer mutant 1.17
K14S X-dimer mutant 1.04
Y142R X-dimer mutant 1.30
W2A K14E Double mutant monomer
W2F Reduced strain on A*/A strand 0.41 [17]
Ala inserted between 2 and 3 Reduced strain on A*/A strand 0.07
AlaAla inserted between 2 and 3 Reduced strain on A*/A strand 0.51
E11D Enhanced strand-swapping 1.40
P5A P6A Swapping strand stabilization 27
P5S P6S Swapping strand stabilization 34
P5G P6G Swapping strand stabilization 37
P5A Swapping strand stabilization 34
P5G Swapping strand stabilization 21
Mouse N-cadherin EC1–2
WT Wild Type 3.88 [4]
P5A P6A Swapping strand stabilization 27 [17]