Table 3. Effects of D2O on Biomolecular Self-Assemblya.
| protein | method | effect |
|---|---|---|
| Escherichia coli protein BirA50 | SE | increased binding energy, KH2Odim/KD2Odim ≈ 10 |
| androgen receptor36 | NMR, DLS, microscopy | enhanced condensation, larger condensates 25 °C shift of cloud point at a H2O/D2O fraction of 1:1 |
| κ-carrageenan25 | rheology | faster assembly, higher elastic modulus, G′D2O/G′H2O ≈ 1.1–1.2 |
| gelatin37 | U-tube, rheology | faster assembly, higher shear modulus, rD2O/rH2O ≈ 2.5, GD2O/GH2O ≈ 3 |
| casein38b | rheology | faster assembly, higher elastic modulus: Gel.On.D2ORG = 9.1 ± 0.1 min; Gel.On.H2ORG = 14.6 ± 0.1 min; Gel.On.D2OTG = 1.3 ± 0.4 min; Gel.On.H2OTG = 11.3 ± 1.1 min; G′D2ORG = 1636.7 ± 75.7 Pa; G′H2ORG = 1183 ± 55.1 Pa; G′D2OTG = 504 ± 27.7 Pa; G′H2OTG = 210 ± 26 Pa |
| insulin39 | 2DIR, IR, Fl | slower assembly, τH2Olag ≈ 16 h; τD2Olag ≈ 20 h |
| α-synuclein40 | Fl, NMR, SANS | faster assembly, τH2Olag ≈ 34 h; τD2Olag ≈ 23 h (0.150 M NaCl) |
| actin52 | static light scattering | formation of multifilament bundles in D2O, DCRD2O(70%)/DCRH2O ≈ 2.5 |
| agarose33 | turbidity | change in the network, τD2O/τH2O ≈ 1.1–1.3 |
| pectin41 | SAXS | change in network fractal dimension |
a
Abbreviations: Kdim = equilibrium dissociation constant for dimerization; τlag= lag time; G′ = elastic modulus at a frequency of 1 Hz; r = rate of initial gelation; G = shear modulus; DCR = derived count rate (light-scattering intensity); Gel.On. = gelation onset; τ = initial turbidity; SE = sedimentation equilibrium measurements; 2DIR = two-dimensional infrared spectroscopy; SAXS= small angle X-ray scattering; SANS = small-angle neutron scattering.
b
Two methods were used to induce gelation, referred to as RG and TG.