Premium
Identification of post‐translationally modified proteins in proteome studies
Author(s) -
Sickmann Albert,
Marcus Katrin,
Schäfer Heike,
ButtDörje Elke,
Lehr Stefan,
Herkner Armin,
Suer Silke,
Bahr Inke,
Meyer Helmut E.
Publication year - 2001
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200105)22:9<1669::aid-elps1669>3.0.co;2-7
Subject(s) - proteome , identification (biology) , computational biology , drug discovery , proteomics , mass spectrometry , gel electrophoresis , two dimensional gel electrophoresis , chemistry , biology , biochemistry , chromatography , gene , botany
Proteome studies are powerful tools to solve many different problems in metabolism, signal transduction, drug discovery, and other areas of interest in life sciences. Up to now, high‐sensitive methods for protein identification after two‐dimensional gel electrophoresis using mass spectrometry are available. However, the identification of post‐translational modifications after two‐dimensional gel electrophoresis is still an unsolved problem. In this paper, we want to give several examples for the successful identification of post‐translational modifications and point mutations.