title: From genome to function: analysis of multi-protein complexes and protein phosphorylation.
abstract: The analysis of multi-protein complexes has seen a tremendous advance with the advent of fast and sensitive mass spectrometric methods for protein identification. However, only specific and sensitive protein purification methods on the front end and detailed bioinformatic sequence analysis of the identified components, allow an efficient route from a DNA sequence to the function of a protein in a complex assembly. Since phosphorylation is one factor which regulates not only activity, but also stability and the ordered association and dissociation of protein complexes, it is necessary to investigate which factors are phosphorylated and where the phosphate moiety is located in the sequence. In this review, analysis of multi-protein complexes and protein phosphorylations are discussed.
authors.affiliation: Protein and Peptide Group, European Molecular Biology Laboratories, Meyerhofstrasse 1, Heidelberg, Germany. neubauer@embl-heidelberg.de
authors.forename: G
authors.initials: G
authors.lastname: Neubauer
authors.forename: M
authors.initials: M
authors.lastname: Wilm
mesh_terms: D023281:Genomics / Q000379:methods*; D006801:Humans; D013058:Mass Spectrometry; D046912:Multiprotein Complexes / Q000032:analysis / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D020543:Proteome / Q000032:analysis* / Q000378:metabolism; D040901:Proteomics / Q000379:methods*
chemical_list: D046912:Multiprotein Complexes; D020543:Proteome