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. We are continuing our studies on the structures and mechanisms of molecular chaperone proteins which, broadly speaking, facilitate the correct folding, assembly and targeting of proteins and RNA molecules in cells. Systems that are currently under study include a 'prokaryotic proteasome'--a 850 kDa complex that is a simple homolog of the eukaryotic proteasome; a family of 'stress endurance' factors called universal stress proteins; a chaperone that facilitates folding and assembly of membrane proteins in bacteria; and a family of RNA chaperones/helicases that modulate RNA structure in cells. Additionally, we are continuing our studies on the structure and mechanism of small catalytic RNAs, or ribozymes.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-27
Application #
7370353
Study Section
Special Emphasis Panel (ZRG1-BPC-E (40))
Project Start
2006-03-01
Project End
2007-02-28
Budget Start
2006-03-01
Budget End
2007-02-28
Support Year
27
Fiscal Year
2006
Total Cost
$855
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
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Niedzialkowska, Ewa; Mruga?a, Beata; Rugor, Agnieszka et al. (2017) Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization. Protein Expr Purif 134:47-62
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