This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Histone posttranslational modifications include reversible acetylation and phosphorylation, methylation, ubiquitinylation and ribosylation with varying stoichiometry at multiple sites. It is thought that certain patterns of modifications at specific amino acid residues encode a language that is read by proteins involved in management of chromatin s many functions. To decipher such a code will require the complete delineation of all posttranslational modifications of each isoform and variant as well as their temporal changes as a function of cell state. This challenge requires development of mass balance for unambiguous delineation of posttranslational status for each particular isoform. It is envisaged that both FTMS together with a dissociation strategy is essential, such as electron capture dissociation or possibly IR activation as well as independent. Digestion and peptide sequence to fill in any gaps in the template derivable from intact Protein dissociation. It is also envisaged that separation of homogenous intact isoforms will have to be separated by mass spectral strategies based on accurate selection of individual molecular weights from mixtures.
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