. Author manuscript; available in PMC: 2014 Jun 3.

Published in final edited form as: Mol Pharm. 2013 May 2;10(6):2311–2322. doi: 10.1021/mp300665u

Table 2.

Oxidation prone amino acid residues and oxidized amino acid detected in peptides derived from oxidized IFNβ1a.¹

Methionine	Phenylalanine	Tyrosine	Tryptophan	Histidine

1	8	3	22	93^*
36	15	30	79^#	97^*
62	38	60	143^#	121^*
117	50	92		131
	67	125		140
	70^#	126
	111	132
	154^#	138
	156	155
		163

Bold numbers: oxidized residues; bold underlined numbers: oxidized residues involved in H-bond critical for the correct folding of IFNβ1a; underlined numbers: residues involved in H-bond critical for the correct folding of IFNβ1a (Karpusas et al.⁷); plain italic numbers: non-oxidized residues.

Hydrophobic residues that stabilize the core of the molecule.

Residues that coordinate a zinc ion, responsible for dimer formation.