Consider the protonated tetrapeptide,
[NH2R1(C=O)NHR2(C=O)NHR3(C=O)NHR4(C=O)OH + H+]+
where R1, R2, R3 and R4 correspond to the residual masses of the aminoacids (AA), i.e., AA mol. weight minus NH2 minus COOH.
Fragmentation of the [Tetrapeptide + H+]+ can give a series of b-ions and a series of y-ions, as below.
b-ions are formed from the N-terminus
b1 NH2R1C=O+
b2 NH2R1C=ONHR2C=O+
b3 NH2R1C=ONHR2C=ONHR3C=O+
The m/z difference between b2 and b1 is then NHR2C=O+, etc..
y-ions are formed from the C-terminus
y1 +NH3R4COOH
y2 +NH3R3CONHR4COOH
y3 +NH3R2CONHR3CONHR4COOH
The m/z difference between y2 and y1 is then R3C=ON+, etc..
NOTES
1. If ALL sequence ions are present, then the polypeptide can be sequenced completely (cannot distinguish Leu/Ile)
2. Sequence ions may also lose small neutrals (e.g.,H2O, NH3, CO) to give an accompanying ion at 18, 17 or 28 lower m/z than the sequence ion
INTERPRETATION
1. Construct, as a reference, a table (Table 1) of the NHRC=O+ values for all 20 common AA's.
2. Assume that m/z 875 is [M+H]+ (NB. it may be a "b" or "y" type ion from a larger peptide !!!)
3. MW 874.5 is consistent with an ≈ 8/9-residue polypeptide.
4. Start at either low or high m/z end of spectrum; construct a table (Table 2) of the m/z difference between adjacent m/z values.
5. Compare the values from Table 2 with those from Table 1.
6. On a copy of the spectrum, pencil in the m/z differences between adjacent signals, and from step 5 annotate on the spectrum the possible AA that is indicated.
7. Assign m/z values as "b" or "y" type ions; e.g., m/z 86 can be either y1 (+NH3R≈8/9COOH) or b1 (NH2R1C=O+).
Good Luck.