Skip to main content
. Author manuscript; available in PMC: 2020 Jul 13.
Published in final edited form as: Biochemistry. 2017 Apr 3;56(14):2061–2070. doi: 10.1021/acs.biochem.7b00067

Table 1.

ZASP and Subdomains: Some Biophysical Parameters

Mw (kDa)c
proteina His-tagb sequence AUC speedd (rpm, × 103) ν-bare (g/cm3) A280f affinityg Kd (M)
ZASP-LΔex10 N24 69.37 60.0 (±1.3) 14.5 0.724 0.95 3.9 × 10−8
ZASP-S WT N21 16.5 2.0 × 10−9
ZASP-S WT none 31.21 29.5 (±0.2) 18.5 0.730 0.77 6.2 × 10−8
2.5 × 10−8h
ZASP-S 147 none 31.5 (±0.8) 18.5 7.6 × 10−8
ZASP-S 165 none 27.3 (±0.3) 18.5 4.4 × 10−8
ZASP-S 268 none 29.18 2.4 × 10−8
ZASP-S 1−251 none 27.00 0.68 2.5 × 10−8
ABRΔ10 WT N34 24.17 26.0 (±1.3) 18.5 0.718 0.58 4.0 × 10−7
ABRΔ10 147 N34 33.6 (±0.8) 18.5 2.6 × 10−7
ABRΔ10 165 N34 25.0 (±2.0) 18.5 1.0 × 10−6
ABRΔ10 WT N21 22.80 24.4 (±1.0) 20.0 0.718 0.58 4.6 × 10−7
3.6 × 10−8i
ABR+10 WT N21 28.62 28.9 (±0.2) 18.5 0.720 0.50 1.0 × 10−5
a

The proteins indicated are either wild-type sequence (WT) or the mutants A147T, A165V and R268C.

b

N-terminal His-tags: N21 = MGSSHHHHHHSSGLVPRGSHM, N24 = HHHHHHDYDIPTTENLYFQGAMGS, N34 = MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRIP.

c

The molecular weights of the constructs as derived from the gene sequence and determined (with error indicated) under native conditions by sedimentation equilibrium (AUC).

d

The speeds used for AUC analysis.

e

The partial specific volumes (ν-bar) were calculated from the amino acid compositions.

f

Absorbance was calculated from amino acid composition: values indicated are A280 nm of 1 mg/mL protein using a 1 cm path-length cell.

g

The binding of the proteins to immobilized G-actin was measured using SPR (Biacore). The binding affinities are given as dissociation constants (Kd) and are in molar (M) units.

h

Affinity determined with ZASP-S immobilized and G-actin as the analyte.

i

Affinity determined by titration calorimetry.