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. Author manuscript; available in PMC: 2016 Apr 1.
Published in final edited form as: Mol Biosyst. 2015 Apr;11(4):1156–1164. doi: 10.1039/c4mb00688g

Table 2.

Disulfide-linked peptides from RNase A identified in this study. The “No. of matches” column represents the number of unique disulfide-linked peptides that support each disulfide bond. The numbers of spectra matched to each peptide are shown according to trypsin treatment time (3, 6, and 24 hrs). For the Cys65–Cys72 bond, intra-disulfide linked peptides were observed including missed cleavages in 3-hr and 6-hr trypsin samples.

Disulfide bond No. of matches Disulfide–linked peptide MW calculat ed No. of spectra
Tryp 3hrs Tryp 6hrs Tryp 24hrs
C26–C84 4 SSTSAASSSNYCNQMMK – CR 2070.8228 2 6 7
QHMDSSTSAASSSNYCNQMMK – CR 2582.0077 2 2
SSTSAASSSNYCNQMMK – CRETGSSK 2660.0935 1 1
QHMDSSTSAASSSNYCNQMMK – CRETGSSK 3171.2784 1
C40–C95 9 CKPVNTFVHESLA – YPNCAYK 2299.0765 10 10 11
CKPVNTFVHESLAD – YPNCAYK 2414.1035 6 8 9
RCKPVNTFVHESLA – YPNCAYK 2455.1776 6 6 6
CK – YPNCAYK 1104.4732 2 3 3
RCK – YPNCAYK 1260.5743 3 3 3
DRCK – YPNCAYK 1375.6013 4 4 1
CKPVNTFVHESLA – ETGSSKYPNCAYK 2888.3473 1
CK – YPNCAYKTTQANK 1747.8022 3
CKPVNTFVHESLA – YPNCAYKTTQANK 2942.4055 1
C65–C72 4 NVACK – NGQTNCYQSYSTMSIT 2327.9821 8 6 5
NVACK – NGQTNCYQSYSTMSITD 2443.009 7 7 10
NVACKNGQTNCYQSYSTMSIT 2309.9715 3 2
NVACKNGQTNCYQSYSTMSITD 2424.9985 1 2
C58–C110 9 VQAVCSQK – HIIVACEGNPYVPVHF 2653.3145 21 27 46
VQAVCSQK – HIIVACEGNPYVPVHFD 2768.3414 23 35 65
VQAVCSQK – HIIVACEGNPYVPVHFDASV 3025.4789 13 23 42
VQAVCSQK – TTQANKHIIVACEGNPYVPVHF 3296.6434 7 5 1
VQAVCSQK – TTQANKHIIVACEGNPYVPVHFD 3411.6703 10 10 2
DVQAVCSQK – HIIVACEGNPYVPVHFD 2883.3683 1 3
PVNTFVHESLADVQAVCSQK – HIIVACEGNPYVPVHF 3962.9447 9 12 6
PVNTFVHESLADVQAVCSQK – HIIVACEGNPYVPVHFD 4077.9716 10 10 13
PVNTFVHESLADVQAVCSQK – HIIVACEGNPYVPVHFDASV 4335.1092 4 9 12