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. 2009 Jan 16;284(3):1652–1663. doi: 10.1074/jbc.M804218200

TABLE 1.

Hydrodynamic properties of recombinant ASAP1 determined by sedimentation velocity experiments BAR-PZA and BAR-PH are the homology models shown in the Fig. 1A. BAR_PZA assumes a bead-on-a-string arrangement for the BAR and PZA segments of ASAP1. BAR_PH assumes a bead-on-string arrangement for the BAR and PH domains. BARP_ZA assumes that the BAR and PH domains form a bead and that ZA forms a second bead. BAR_P_ZA assumes that BAR, PH, and ZA are each beads on the string.

Protein swa s20,wb shc f/fod Axial dimensionse
BAR-PZAf 5.1 5.9 6.6 1.82 32.8 × 3.3
BAR_PZA 5.9
BARP_ZA 5.9
BAR_P_ZA 5.3
BAR-PHf 3.9 4.5 4.8 1.73 24.9 × 3.0
BAR_PH 4.2
PZA 2.8 3.2 3.6 1.44 11.9 × 2.9
ZA 2.4 2.7 2.9 1.36 8.8 × 2.9
a

Weight average sedimentation coefficient at experimental conditions

b

Corrected to standard conditions (water, 20 °C)

c

Sedimentation coefficient determined for homology model using Hydropro7

d

Frictional ratio obtained with s20,w and molar mass using SEDNTERP

e

Axial dimensions (nm) of cylinder model (length × diameter) assuming hydration level of 0.3 g of water/gram of protein

f

These domains were present exclusively as dimers in solution above 0.1 mg/ml (1 μm)