Relative peak areas of a
LLYLR and b
YLR and photomodifications of these after UVA irradiation: 1 Y + O; 2 Y + 2O; 3 Y + O–2H; 4 Y + 2O–2H; 5 Y + N + 2O–H. Spectra peak areas are internally weighted, and the relative abundance of the peak area of the unmodified peptide at zero time is defined as 1.0. Error bars represent standard errors of the mean (±SEM)
Peptides containing tryptophan residues (Figs. 2, 3) were
observed to be modified considerably more rapidly than those
containing tyrosine residues (Figs. 4, 5), as evidenced
by greater and more definite decreases in parent peptides and
larger increases in modified products. .
This was demonstrated by the tyrosine degradation profiles;
sensitive MS/MS characterisation confirmed the presence of tyrosine
photoproducts (indicating the degradation of tyrosine residues),
whereas abundance profiling shows the majority of tyrosine
photoproducts to be present at very low abundance (evidenced by
maximum product levels only 10% as abundant as unmodified parent at
zero time, and by large measurement errors), to the point that most
are probably unsuitable for use as quantitative damage markers
using this technique (Figs. 4, 5).
Viewing this image requires a subscription. If you are a subscriber, please log in.
This image is from the article titled "Profiling of residue-level photo-oxidative damage in peptides"
(from Amino Acids), which is copyrighted by Springer-Verlag. For more information on the
copyright for this image, please refer to the full image caption and to the
The image is being made available for non-commercial purposes for subscribers to SpringerImages. For more information on what you are allowed to do with this image, please see our copyright policy.
To request permissions to use any copyrighted material, please visit the source document.
Report a copyright concern regarding this image.
Log in or register to save your favorite images and download them as high-quality PowerPoint or PDF files.
Log in or register to save your search criteria.
© Springer, part of Springer Science+Business Media.
Remote Address: 18.104.22.168 Server: 18