Table 2.

Predicted interaction scores and experimentally measured stabilities of triple-helix formation for mixtures of peptides A, B, C at pH 1.0 and 7.0, respectively. Scores and apparent T_m of species showing cooperative unfolding are highlighted in bold.

Mixture	Scorea			Apparent Tm
	pH 7.0		pH 1.1	pH 7.0d
	Eq. 1	Eq. 2	Eq. 2	preheatedb	not preheated
A	20	9	0	N/A	N/A
B	30	18	10	N/A	N/A
C	29	20	8	N/A	N/A
A:2B	−7	−3	2	20	20
2A: B	−7	−7	0	20	19
B:2C	−5	−4	2	N/Ac	N/Ac
2B:C	−6	−3	2	22	20
A:2C	2	17	4	N/A	N/A
2A:C	−2	14	2	N/A	N/A
A:B:C	−29	−4	0	20	19

^athe lowest scores among the scores of the species with the same mixing ratio of peptides but different staggering phases such as AAB, ABA, and BAA are shown.

^bbefore incubation at 0 °C for 2–3 days, the mixtures are incubated at 40 °C for 15 min.

^cThermal melting performed after elimination of white precipitates by centrifugation.

^dNo triple-helical structure observed for any mixture at pH 1