Table 2. Effects of D₂O on the Properties of Proteins and Other Biomolecules^a.

biomolecule	method	effect
bovine serum albumin18	DSC	enhanced stability of the native state, TD2Od – TH2Od ≈ 2–3 °C
bovine serum albumin19	CD	enhanced stability of the native state Irr. TD2Od – Irr. TH2Od ≈ 8 °C
bovine serum albumin20	DLS, Fl, UV–vis, SE-HPLC	enhanced stability of the native state monomer % at 65 °C: 85% in D2O, 75% in H2O
lysozyme18	DSC	enhanced stability of the native state, TD2Od – TH2Od ≈ 2–3 °C
tubulin21	CD, DSC, Fl	enhanced stability of the native state, TD2Od – TH2Od ≈ 3 °C
acyl carrier proteins22	NMR	enhanced stability of the native state, ΔGD2ON→U = 2.3 kcal/mol; ΔGH2ON→U = 1.8 kcal/mol
collagen peptides24	CD, DSC	enhanced stability of the folded state, TD2Om – TH2Om ≈ 4 °C
ribonuclease A27	DSC	enhanced stability of the native state, TD2Om – TH2Om ≈ 4 °C
Drosophila signal transduction protein26	NMR	enhanced stability of the folded state, TD2Om – TH2Om ≈ 12 °C
κ-carragenean25	DSC	enhanced stability of the folded state, TD2Ogel→liq – TH2Ogel→liq ≈ 3 °C
elastin-like peptides28	DSC, CD, IR	enhanced stability of the collapsed state, Propensity to form β-turn/β-aggregate, LCSTH2O – LCSTD2O ≈ 2–5 °C
peptides containing alanine29	CD	propensity for PPII structure: 5–200% higher PPII signal in D2O
plastocyanin32	MD	altered solvent–protein interactions: 10–30% reduction of protein–water H-bonds
test polypeptides34	MD	altered solvent–protein interactions
agarose (Ag2)33	NMR	lower solvent–polysaccharide affinity, NH2Ow/ND2Ow ≈ 3.8
ribonuclease T131	luminescence	increased protein rigidity, IPLD2O = 36 ms, IPLH2O = 28 ms
β-lactoglobulin31	luminescence	increased protein rigidity, IPLD2O = 44 ms, IPLH2O = 30 ms
liver alcohol dehydrogenase31	luminescence	increased protein rigidity IPLD2O = 819 ms, IPLH2O = 630 ms
alkaline phosphatase31	luminescence	increased protein rigidity, IPLD2O = 2142 ms, IPLH2O = 2060 ms
apo-azurin31	luminescence	increased protein rigidity IPLD2O = 603 ms, IPLH2O = 564 ms
TAS1R2/TAS1R3 receptor30	MD	smaller radius of gyration RD2Og is ≈3% smaller than RH2Og
azurin,35 lactoglobulin, ribonuclease	MD	smaller radius of gyration RD2Og is ≈1% smaller than RH2Og

^aAbbreviations: T_d = denaturation temperature; Irr. T_d = irreversible denaturation temperature; T_m = melting temperature of the native state; T₀ = transition temperature from folded-to-unfolded; R_g = radius of gyration; IPL = intrinsic Trp phosphorescence lifetime; ΔG_N→U = Gibbs energy of unfolding; T_gel→liq = gel-to-liquid transition temperature; LCST = lower critical solution temperature; N_w = number of hydration waters per mass unit of agarose; DSC = differential scanning calorimetry; SE-HPLC = size exclusion high-performance liquid chromatography; CD = circular dichroism; DLS = dynamic light scattering; Fl = fluorescence measurements; NMR = nuclear magnetic resonance; MD = molecular dynamics simulations.

Part of this table is taken from ref (26).