-
Characterization by tandem mass spectrometry of structural modifications in proteins.
Tandem mass spectrometry can be used to solve a number of protein structural problems that are not amenable to conventional methods for amino acid sequencing. Typical problems that use this approach involve characterization of peptides with blocked amino termini or peptides that have been otherwise posttranslationally processed, such as, by phosphorylation or sulfation. The structure and homogeneity of synthetic peptides can also be evaluated. Since peptides can be selectively characterized in the presence of other peptides or contaminants, the need for extensive purification is reduced or eliminated.
PMID: 3303336 [PubMed - indexed for MEDLINE]
-
Cited by 13 PubMed Central articles
-
Protein-Sequence Polymorphisms and Post-translational Modifications in Proteins from Human Saliva using Top-Down Fourier-transform Ion Cyclotron Resonance Mass Spectrometry.
Whitelegge JP, Zabrouskov V, Halgand F, Souda P, Bassilian S, Yan W, Wolinsky L, Loo JA, Wong DT, Faull KF.
Int J Mass Spectrom. 2007 Dec 1; 268(2-3):190-197.
[Int J Mass Spectrom. 2007]
-
Biomarkers in newly diagnosed pediatric-extensive chronic graft-versus-host disease: a report from the Children's Oncology Group.
Fujii H, Cuvelier G, She K, Aslanian S, Shimizu H, Kariminia A, Krailo M, Chen Z, McMaster R, Bergman A, et al.
Blood. 2008 Mar 15; 111(6):3276-85. Epub 2007 Oct 9.
[Blood. 2008]
-
The RESID database of protein structure modifications: 2000 update.
Garavelli JS.
Nucleic Acids Res. 2000 Jan 1; 28(1):209-11.
[Nucleic Acids Res. 2000]
- » See all...