This subproject is one of many research subprojects utilizing the resources provided by a Shared Instrumentation 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 grant, which is not necessarily the institution for the investigator. DESCRIPTION (provided by applicant): We are applying for a Shared Instrumentation Grant to purchase a BIACORE T100 surface plasmon resonance instrument, which will be used to measure molecular interactions in vitro. Four major users have projects studying: molecular intractions in RNA trafficking, ankyrin repeat protein interactions, protein-protein interactions in secretory granule formation and molecular interactions in herpes virus replication. Three minor users have projects studying: protein-protein interactions in bacterial cell division, molecular interactions in DMA mismatch repair and molecular interactions in bacterial pilus formation. Each of the major and minor investigators have experience analzying molecular interactions by conventional techniques. However, their individual projects will benefit by the capability of the BIACORE T100 instrument to directly measure kinetic binding constants. The quantitative data provided by the BIACORE T100 will be used as input parameters for computational models of specific cell biological systems. Thus, the BIACORE T100 represents an enabling technology for computational modeling of cell biological processes. This work will further human health as most, if not all, cell biological processes are mediated by networks of reversible molecular interactions. Diseases such as cancer, multiple sclerosis and Alzheimer's disease are caused by disruption of specific interaction networks. In order to understand how a particualr interaction network functions it is necessary to know how rapidly each molecule in the network binds to its partners and how rapidly they dissociate. The instrument we are requesting, the BIACORE T100, will enable us to directly measure how rapidly individual molecules associate and dissociate. This quantitative information will enable us to understand how molecular interaction networks mediate specific cell biological processes and how such networks are disrupted in disease

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR022624-01
Application #
7335302
Study Section
Special Emphasis Panel (ZRG1-IMM-G (30))
Project Start
2006-04-15
Project End
2007-04-14
Budget Start
2006-04-15
Budget End
2007-04-14
Support Year
1
Fiscal Year
2006
Total Cost
$224,000
Indirect Cost
Name
University of Connecticut
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
022254226
City
Farmington
State
CT
Country
United States
Zip Code
06030
Chen, Yan; Bai, Ping; Mackay, Shannon et al. (2011) Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation. J Virol 85:968-78
Levin, Mikhail K; Hingorani, Manju M; Holmes, Raquell M et al. (2009) Model-based global analysis of heterogeneous experimental data using gfit. Methods Mol Biol 500:335-59
Gao, Yuanzheng; Tatavarty, Vedakumar; Korza, George et al. (2008) Multiplexed dendritic targeting of alpha calcium calmodulin-dependent protein kinase II, neurogranin, and activity-regulated cytoskeleton-associated protein RNAs by the A2 pathway. Mol Biol Cell 19:2311-27
Carson, John H; Gao, Yuanzheng; Tatavarty, Vedakumar et al. (2008) Multiplexed RNA trafficking in oligodendrocytes and neurons. Biochim Biophys Acta 1779:453-8
Paradise, Allison; Levin, Mikhail K; Korza, George et al. (2007) Significant proportions of nuclear transport proteins with reduced intracellular mobilities resolved by fluorescence correlation spectroscopy. J Mol Biol 365:50-65