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).

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR000954-33
Application #
8168769
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (40))
Project Start
2010-03-10
Project End
2010-12-31
Budget Start
2010-03-10
Budget End
2010-12-31
Support Year
33
Fiscal Year
2010
Total Cost
$616
Indirect Cost
Name
Washington University
Department
Internal Medicine/Medicine
Type
Schools of Medicine
DUNS #
068552207
City
Saint Louis
State
MO
Country
United States
Zip Code
63130
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