Figure 2 | Scientific Reports

Figure 2

From: Identification and physical characterization of a spontaneous mutation of the tobacco mosaic virus in the laboratory environment

Figure 2

(A) Deconvoluted ESI–MS data of denatured TMV samples showing distribution between wTMV and mTMV. One sample contains 60% wTMV and 40% mTMV, while the other sample is almost entirely mTMV. (B) Peptide spectra recovered using the wild-type coat protein sequence. Peptide 142–158 (left) comes from a tryptic digest. Peptide 151–158 (right) comes from a peptic digest. Both peptides are reduced in the mTMV sample compared to the mixture of wTMV and mTMV. (C) Peptide spectra recovered using coat protein sequence containing S at position 155. Both peptides are more abundant in the mTMV sample compared to the mixture of wTMV and mTMV. (D) Fragmentation data for C-terminal peptides from the mTMV digests (top is trypsin; bottom is pepsin) when data was searched using a coat protein sequence containing the G155S mutation.

Back to article page