A comparison between a resolving power of 15K and 45K at all three column temperatures was performed to determine if increased MS resolving power could improve detection of full-length AAV VPs and their proteoforms. Data deconvolution was performed using BioPharma Finder (BPF) Version 4.1, where the three replicate injections at each condition (column temperature and MS resolving power) were processed together (see Table for BPF processing parameters). Results were filtered as described in Section 2.8 to ensure all identifications were valid. Proteoform identifications were assigned using the PTMs identified in Section 3.1. .0 * Poor identification due to high background interference from mobile phase ^ Identifications were found in a minimum of two of the replicates instead of all three replicates -Feature was not identified during analysis Analysis of deconvoluted data in BPF revealed the advantages and disadvantages of using increased MS resolving power for VP proteoform identification (Table ). With an MS resolving power of 45K, separation at 25°C resulted in the detection of VP1, VP2, and VP3 all unmodified, oxidized VP1 (VP1-Ox), oxidized VP2 (VP2-Ox), oxidized VP3 (VP3-Ox), VP3 containing 2 oxidations (VP3-2Ox), and the A211(Ac)-VP3 variant. A mass of VP3 minus ≈19.5 Da (VP3 -≈19.5 Da) was also clearly detected. As explained later, this mass most likely represents the presence of succinimide D formed from Asp. For separations performed at 45°C, the same proteoforms as 25°C were identified except for A211(Ac)-VP3 and at 60°C all proteoforms except A211(Ac)-VP3 and oxidized VP2 were identified. The reduction of identifications for separations performed at 45°C and 60°C with a MS resolving power of 45K is the result of the reduced signal intensity due to increased MS resolution combined with reduced chromatographic resolution that occurs when separation is performed at higher column temperatures. With an MS resolving power of 15K, unmodified VP1, VP1-Ox, VP2, VP2-Ox, VP3, VP3-Ox, and A211(Ac)-VP3 were identified in separations performed at all three column temperatures. The high matched mass error (mme) for the oxidized VPs is a result of background interference from ions in the mobile phase. Additionally, a feature with a mass of 60173.24 Da was detected during deconvolution analysis of the separations performed at 60°C, though identification could not be determined based on peptide mapping results. Deconvolution analysis revealed this feature to elute at approximately 19.41 minutes (mean apex retention time) with a relative abundance of 1.35%.