Table 7.

TRF as pyro-glu-his-pro amide.

T = the TRF peptide is protected at both the N- and C-terminal ends as pyro-glu-his-pro-amide
~T = TRF is pyro-glu-his-pro
E1 = when the glutamic acid end is amidated it has the tendency to form the internal ring known as pyro-glu
E2 = the amide form of pyro-glu-his-pro is analogous to other biologically active polypeptides
E3 = a comparison of purified TRF vs. synthetic pyro-glu-hist-pro-amide by mass spectroscopy showed them to be identical
E4 = purified TRF and synthetic pyro-glu-his-pro-amide could not be distinguished in 17 different chromatographic systems and assays
Probability	Value	Code	Description
P(T)=	0.84		Posterior of pyro-glu-his-pro
P(~T)=	0.16		1—prior
P(E1|T)=	0.6	WC	Pyro-glu-his-pro-amide is weakly consistent with amidation
P(E1|~T)=	0.4	WI	Amidation is weakly inconsistent with TRF as pyro-glu-his-pro
P(E2|T)=	0.6	WC	The amide form of TRF is weakly consistent with other biologically active peptides
P(E2|~T)=	0.4	WI	TRF as pyro-glu-his-pro is weakly inconsistent with other biologically active peptides
P(E3|T)=	0.7	SC	Mass spectroscopy of TRF showed fragments strongly consistent with pyro-glu-his-pro-amide
P(E3|~T)=	0.3	SI	Mass spectroscopy of TRF showed fragments strongly inconsistent with pyro-glu-his-pro
P(E4|T)=	0.7	SC	The indistinguishability of pyro-glu-his-pro-amide from natural TRF across chromatographic tests is strongly consistent with their equivalence
P(E4|~T)=	0.3	SI	The ability of pyro-glu-his-pro to be distinguished from natural TRF by chromatographic tests is strongly inconsistent with their equivalence
P(T|E1-E4)=	0.99	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.