. 2016 Oct 18;2(11):812–819. doi: 10.1021/acscentsci.6b00205

Table 1. Plateau Moduli, G(t = 0) and G(t → ∞), and Characteristic Relaxation Time, <τ>, for EPE and the Six Single-Site Mutant Variants Were Determined by Fitting the Data to a Stretched Exponential Model^a.

protein	<τ> (s)	G(t = 0) (kPa)	G(t → ∞) (kPa)	M_c (t → ∞) (kg mol^–1)
L37A	0.22 ± 0.13	6.9 ± 0.6	4.7 ± 1.0	28.1
L37V	1.02 ± 0.14	12.1 ± 0.4	5.1 ± 0.1	28.2
I58A	1.70 ± 0.15	11.1 ± 0.1	4.5 ± 0.3	32.0
L37I	9.83 ± 1.19	13.6 ± 0.4	5.2 ± 0.7	30.4
EPE	134 ± 8	14.0 ± 0.6	4.6 ± 0.2	32.3
T40A	762 ± 62	14.7 ± 0.2	5.7 ± 0.6	26.5
Q54A	1608 ± 135	14.8 ± 0.9	6.8 ± 0.8	23.0

L37A was not well fit by a stretched exponential model, so the single exponential model is reported instead (n = 3, avg ± s.d.). The equilibrium modulus G(t → ∞) was used to determine the average molecular weight between covalent cross-links (M_c). The expected value of M_c based on the protein molecular weight and the molecular weight of two arms of the PEG-4VS cross-linker is 26.5 kg mol^–1.

Table 1. Plateau Moduli, G(t = 0) and G(t → ∞), and Characteristic Relaxation Time, <τ>, for EPE and the Six Single-Site Mutant Variants Were Determined by Fitting the Data to a Stretched Exponential Modela.

Table 1. Plateau Moduli, G(t = 0) and G(t → ∞), and Characteristic Relaxation Time, <τ>, for EPE and the Six Single-Site Mutant Variants Were Determined by Fitting the Data to a Stretched Exponential Model^a.