INTRINSICALLY DISORDERED PROTEINS AND MASS SPECTROMETRY

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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. Protein folding, protein dynamics, protein structure/function relationships, protein-protein interactions and polymerization/aggregation mechanisms are projects currently under study in this laboratory. The Frieden laboratory is particularly interested in measuring the kinetics of side chain packing and stabilization during folding as well as dynamics in the unfolded state. They are also studying the dynamics and aggregation properties of intrinsically disordered proteins including AB, polyglutamine (alone and in huntingtin Exon1) and CsgA. CsgA is a bacterial protein secreted into the media forming fibrils that surround the bacteria. Studies include the behaviour of proteins unfolded by denaturant. The main methods for these sutdies include FCS and NMR (after incorporation of fluorine labeled amino acids).