Table 1 Single-molecule force spectroscopy parameters associated with unfolding events of various constructs and additives.

From: Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module

Construct/Additive

Contour length LC (nm)a

Persistence length Lp (nm)a

Unstressed unfolding rate \({k}_{u}^{0}\) (s−1)b

Barrier position \({\gamma }_{u}\) (nm)b

AIM-A1

26.6 ± 0.5

0.60 ± 0.05

0.074 ± 0.021

1.10 ± 0.10

A1-CAIM

13.1 ± 0.9

0.72 ± 0.17

0.093 ± 0.033

2.34 ± 0.29

NAIM-A1

12.9 ± 1.0

0.78 ± 0.22

0.154 ± 0.024

1.22 ± 0.09

AIM-A1 H1268D

17.7 ± 0.9

0.67 ± 0.11

0.288 ± 0.052

0.84 ± 0.12

AIM-A1 R1341Q

14.5 ± 0.3

1.32 ± 0.09

0.27 ± 0.12

1.15 ± 0.29

AIM-A1 with 6G1

14.6 ± 1.0

0.76 ± 0.19

0.10 ± 0.05

1.48 ± 0.28

A1-CAIM with 6G1

13.0 ± 0.6

1.08 ± 0.15

0.096 ± 0.008

3.38 ± 0.08

NAIM-A1 with 6G1

14.2 ± 1.4

0.95 ± 0.37

0.247 ± 0.069

1.17 ± 0.18

AIM-A1 with CR1

27.9 ± 2.2

0.37 ± 0.07

0.133 ± 0.030

0.94 ± 0.10

AIM-A1 with VHH81

25.3 ± 0.8

0.56 ± 0.07

0.0061 ± 0.0032

1.47 ± 0.14

  1. aContour length and persistence length are fitted worm-like chain model parameters. Uncertainties are the standard error of the fits.
  2. bUnstressed unfolding rate and barrier position are fitted Bell–Evans model parameters. Uncertainties are the standard error of the fits.