Home LiteratureArticle Details
PMID: 3303336 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Characterization by tandem mass spectrometry of structural modifications in proteins.

Science (New York, N.Y.) ·Vol. 237 ·No. 4818 ·1987-08-28 ·Pages 992-8

Biemann K, Scoble HA

Abstract

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.

MeSH Terms
Amino Acid Sequence Amino Acyl-tRNA Synthetases Escherichia coli Humans Mass Spectrometry Phosphorylation Protein Processing, Post-Translational Proteins Saccharomyces cerevisiae
Chemicals
Proteins Amino Acyl-tRNA Synthetases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Biemann K
Scoble H A
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1987-08-28
Pages
992-8
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIGMS NIH HHS · GM05472 · United States
NCRR NIH HHS · RR00317 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com