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. 2024 Oct 17. Online ahead of print. doi: 10.1039/d4cs00569d

Thermodynamic data for homoternary complexes.

Host Amino acid, peptide, or protein K ter (M−2) ΔH (kcal mol−1) TΔS (kcal mol−1)
Q8a Tryptophan 6.9 × 107 −17.1 6.3
Q8a Phenylalanine 1.1 × 108 −15.2 4.2
Q8a All 18 other amino acids ndm nrn nr
Q8b H-Trp-Gly-Gly-OH 3.6 × 109 −22.8 9.7
Q8b H-Gly-Trp-Gly-OH nd nr nr
Q8b H-Gly-Gly-Trp-OH nd nr nr
Q8b H-Phe-Gly-Gly-OH 1.5 × 1011 −29.6 14.2
Q8b H-Gly-Phe-Gly-OH nd nr nr
Q8b H-Gly-Gly-Phe-OH nd nr nr
Q8b H-Tyr-Gly-Gly-OH nd nr nr
Q8b H-Gly-Tyr-Gly-OH nd nr nr
Q8b H-Gly-Gly-Tyr-OH nd nr nr
Q8b H-His-Gly-Gly-OH nd nr nr
Q8b H-Gly-His-Gly-OH nd nr nr
Q8b H-Gly-Gly-His-OH nd nr nr
Q8c H-Phe-Gly-Gly-OH 2.3 × 1010 −25.3 11.2
Q8c H-Phe-Gly6-OH 4.4 × 109 −23.0 9.8
Q8d H-Ala-Glu-Phe-Arg-His-NH2 3.0 × 1010 −15.3 0.9
Q8d H-Leu-Val-Phe-Ile-Ala-NH2 7.7 × 109 −9.0 4.5
Q8d H-Val-Ile-Phe-Ala-Glu-NH2 1.6 × 1013 −20.8 2.8
Q8e H-Phe-Leu-NH2 1.9 × 1011 −26.7 11.3
Q8e H-Tyr-Ala-Leu-NH2 8.7 × 107 −18.1 7.3
Q8f H-Phe-Gly-Gly-Gly-Cys-OH 2.3 × 1013 −21.8 6.2
Q8g H-Phe-Gly-Gly-OH 1.7 × 1012 nr nr
Q8h H-Tyr-His-OH 2.4 × 108 nr nr
Q8i mCFP-FGG 2.5 × 1013 −29.3 10.6
Q8j Caspase-9-FGG 2.7 × 1012 −23.7 5.3
Q8k GST-FGG 2.9 × 1012 −13.2 −3.8
Q8l Aβ 4–16 5.5 × 1010 nr nr
Q8l Aβ 1–16 nd nr nr
a

10 mM sodium phosphate, pH 7.0, 300 K.32

b

10 mM sodium phosphate, pH 7.0, 300 K.18

c

PBS: 10 mM sodium phosphate, 1.8 mM potassium phosphate, 137 mM NaCl, 2.7 mM KCl, pH 7.4, 298 K.49

d

10 mM sodium phosphate, pH 7.4, 298 K.50

e

10 mM sodium phosphate, pH 7.0, 298 K.51

f

Pure water, 298 K.52

g

Pure water, 298K.53

h

50 mM sodium acetate, pH 4.74.54

i

Monomeric cyan fluorescent protein modified with N-terminal FGG, 10 mM sodium phosphate, pH 7.0, 303 K.55

j

Caspase-9 modified with N-terminal FGG, 10 mM sodium phosphate, pH 7.0, 303 K.56

k

Glutathione-S-transferase modified with N-terminal FGG, 20 mM sodium phosphate, 1 mM EDTA, pH 7.4, 298 K.57

l

10 mM sodium phosphate, pH 7.4, 298 K.58

m

Not detected.

n

Not reported. Putative binding sites are in bold.