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. 2023 Aug 2;8:1214512. doi: 10.3389/frma.2023.1214512

Table 5.

TRF as an acetylated peptide.

T = the TRF peptide is blocked at the N-terminal by an acetyl group
~T = TRF consists only of the three amino acids: glu, his, and pro
E1 = no NH2 group was found at the N-terminal of the TRF peptide
E2 = in some natural peptides the N-terminal is blocked by an acetyl group (analogy)
E3 = one of the six acetylated combinations of the three amino acids was active using the TRF assay
E4 = the acetylated form was not as active as purified natural TRF
Probability Value Code Description
P(T)= 0.19 Posterior from simple peptide glu-his-pro
P(~T)= 0.81 1—prior
P(E1|T)= 0.7 SC The absence of an NH2 group on the N-terminal is strongly consistent with an acetyl group at the N-terminal
P(E1|~T)= 0.3 SI The absence of an NH2 group on the N-terminal is strongly inconsistent with TRF as a simple peptide
P(E2|T)= 0.6 WC An acetyl group on the N-terminal of TRF is weakly consistent with other natural peptides
P(E2|~T)= 0.4 WI An acetyl group on the N-terminal of a simple peptide is weakly inconsistent with its being a simple peptide
P(E3|T)= 0.7 SC The TRF activity of acetylated glu-his-pro is strongly consistent with TRF having that sequence
P(E3|~T)= 0.3 SI The absence of activity of the glu-his-pro sequence without acetylation is strongly inconsistent with TRF as a simple peptide
P(E4|T)= 0.4 WI The lower activity of acetylated glu-his-pro is weakly inconsistent with it being identical to natural TRF
P(E4|~T)= 0.5 N The lower activity of the acetylated form is neutral to TRF as a simple peptide
P(T|E1-E4)= 0.61 Confirm

In the body of the table prior and posterior probabilities are shaded in yellow. Conditional probabilities are shaded green for the theory being tested and pink for the alternative. Bolded words in the Description column indicate the relationship between the theory and evidence in accord with the abbreviations in the Code column.