Funds are requested to purchase a Bruker ELEXSYS 580 pulse spectrometer capable of running double electron electron resonance (DEER), double quantum coherence (DQC), and electron nuclear double resonance (ENDOR) experiments at cryogenic temperatures. Pulse instrumentation of this kind is not available at the Medical College of Wisconsin (MCW), or in the surrounding regional community. Recent advances in the commercial instrumentation and application of pulsed EPR spectroscopy are rapidly making this technique essential to the site-directed spin labeling (SDSL) and metal EPR research communities. The ability of DEER and DQC methods to measure interspin distances in the range of 15-50? opens up an entirely new range of possibilities in the study of biomedically significant research problems. ? ? Five major users will utilize this instrument to measure long distance ranges within protein or peptide systems. In addition, numerous minor users are identified, each with a need for advanced pulse instrumentation not available in the region. Each major user is NIH-funded and has an established and growing research group dedicated to the advancement of protein structure and functional dynamics. This instrumentation will immediately and significantly advance the productivity of the projects outlined in this proposal in addition to enhancing the research environment for the surrounding community. ? ? Having the pulse capability that this instrumentation will provide is vital to the rapid progress of the discussed NIH-funded projects as well as to providing MCW researchers and visitors access to state-of-the-art EPR instrumentation. ? ? ?

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR022422-01A1
Application #
7210413
Study Section
Special Emphasis Panel (ZRG1-BCMB-K (30))
Program Officer
Tingle, Marjorie
Project Start
2007-03-01
Project End
2008-02-29
Budget Start
2007-03-01
Budget End
2008-02-29
Support Year
1
Fiscal Year
2007
Total Cost
$500,000
Indirect Cost
Name
Medical College of Wisconsin
Department
Biophysics
Type
Schools of Medicine
DUNS #
937639060
City
Milwaukee
State
WI
Country
United States
Zip Code
53226
Schultz, Kathryn M; Klug, Candice S (2018) Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer. Protein Sci 27:381-389
Tessmer, Maxx H; Anderson, David M; Pickrum, Adam M et al. (2018) Identification of a ubiquitin-binding interface using Rosetta and DEER. Proc Natl Acad Sci U S A 115:525-530
Schultz, Kathryn M; Fischer, Matthew A; Noey, Elizabeth L et al. (2018) Disruption of the E. coli LptC dimerization interface and characterization of lipopolysaccharide and LptA binding to monomeric LptC. Protein Sci 27:1407-1417
Chen, Qiuyan; Perry, Nicole A; Vishnivetskiy, Sergey A et al. (2017) Structural basis of arrestin-3 activation and signaling. Nat Commun 8:1427
Suliman, Muna; Santosh, Vishaka; Seegar, Tom C M et al. (2017) Directed evolution provides insight into conformational substrate sampling by SrtA. PLoS One 12:e0184271
Schultz, Kathryn M; Klug, Candice S (2017) High-pressure EPR spectroscopy studies of the E. coli lipopolysaccharide transport proteins LptA and LptC. Appl Magn Reson 48:1341-1353
Mandal, Tirtha; Shin, Seungjin; Aluvila, Sreevidya et al. (2016) Assembly of Bak homodimers into higher order homooligomers in the mitochondrial apoptotic pore. Sci Rep 6:30763
Alvarez, Frances Joan D; Orelle, Cédric; Huang, Yan et al. (2015) Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter. Mol Microbiol 98:878-94
Zhuo, Ya; Vishnivetskiy, Sergey A; Zhan, Xuanzhi et al. (2014) Identification of receptor binding-induced conformational changes in non-visual arrestins. J Biol Chem 289:20991-1002
Schultz, Kathryn M; Feix, Jimmy B; Klug, Candice S (2013) Disruption of LptA oligomerization and affinity of the LptA-LptC interaction. Protein Sci 22:1639-45

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