Nine investigators from three campuses of the University of Maryland seek funding for a Beckman Coulter Optima XL-I analytical ultracentrifuge. The user's group consists of Drs. Beckett (P1), Davis, Isaacs, Julin, Kahn, Munoz, and Greer from the Departments of Chemistry & Biochemistry and Chemical Engineering and the Center for Biological Structure & Organization at UMCP, Dr. David Weber from the Department of Biochemistry and Molecular Biology at the University of Maryland, Baltimore and Dr. Michael Summers from the HHMI and Department of Chemistry & Biochemistry, University of Maryland, Baltimore County. The centrifuge will be used for research in three general areas including analysis of macromolecular assembly in systems of biological interest, determination of the assembly properties of peptides and proteins for folding and high resolution structural studies, and characterization of the energetics and stoichiometries of synthetic biomimetic assemblies. Specific projects include determination of the energetics and stoichiometries of protein-protein interactions in transcriptional regulation and DNA recombination and repair, analysis of model ion channels, and determination of the assembly properties of model peptides for folding studies. The versatility provided by the absorption and interference optics of the Beckman Optima XL-I analytical ultracentrifuge will be essential to the success of the broad range of applications described in this proposal.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR015899-01A1
Application #
6440908
Study Section
Special Emphasis Panel (ZRG1-SSS-2 (04))
Program Officer
Tingle, Marjorie
Project Start
2002-05-01
Project End
2003-04-30
Budget Start
2002-05-01
Budget End
2003-04-30
Support Year
1
Fiscal Year
2002
Total Cost
$214,968
Indirect Cost
Name
University of Maryland College Park
Department
Chemistry
Type
Schools of Earth Sciences/Natur
DUNS #
City
College Park
State
MD
Country
United States
Zip Code
20742
Postel, Sandra; Deredge, Daniel; Bonsor, Daniel A et al. (2016) Bacterial flagellar capping proteins adopt diverse oligomeric states. Elife 5:
Bonsor, Daniel A; Günther, Sebastian; Beadenkopf, Robert et al. (2015) Diverse oligomeric states of CEACAM IgV domains. Proc Natl Acad Sci U S A 112:13561-6
Bonsor, Daniel A; Pham, Kieu T; Beadenkopf, Robert et al. (2015) Integrin engagement by the helical RGD motif of the Helicobacter pylori CagL protein is regulated by pH-induced displacement of a neighboring helix. J Biol Chem 290:12929-40
Eginton, Christopher; Naganathan, Saranga; Beckett, Dorothy (2015) Sequence-function relationships in folding upon binding. Protein Sci 24:200-11
Eginton, Christopher; Beckett, Dorothy (2013) A large solvent isotope effect on protein association thermodynamics. Biochemistry 52:6595-600
Ingaramo, Maria; Beckett, Dorothy (2012) Selectivity in post-translational biotin addition to five human carboxylases. J Biol Chem 287:1813-22
Adikaram, Poorni R; Beckett, Dorothy (2012) Functional versatility of a single protein surface in two protein:protein interactions. J Mol Biol 419:223-33
Hondorp, Elise R; Hou, Sherry C; Hempstead, Andrew D et al. (2012) Characterization of the Group A Streptococcus Mga virulence regulator reveals a role for the C-terminal region in oligomerization and transcriptional activation. Mol Microbiol 83:953-67
Ingaramo, Maria; Beckett, Dorothy (2011) Biotinylation, a post-translational modification controlled by the rate of protein-protein association. J Biol Chem 286:13071-8
Daniels, Kyle G; Beckett, Dorothy (2010) Biochemical properties and biological function of a monofunctional microbial biotin protein ligase. Biochemistry 49:5358-65

Showing the most recent 10 out of 20 publications