We propose to continue the operation of the Biophysics Collaborative Access Team (BioCAT) undulator beamline 18ID at the Advanced Photon Source, Argonne National Laboratory. BioCAT's mission is to provide a national research resource for the study of partially ordered biological molecules, complexes of biomolecules, and cellular structures under conditions similar to those present in living cells. The goal of this research is to understand the detailed mechanisms of action of such systems at the molecular level. Health issues that are directly addressed are function and regulation of skeletal and cardiac muscle;collagenous structures and interactions with collagen binding proteins that have roles in heart disease and cancer;structure of amyloids, neurofibrillary tangles, metal metabolism and relationship to neurodegenerative disease. Basic biomedical questions that are addressed include the structure and dynamics of macromolecular complexes in solution, kinetics of protein and RNA folding, and roles of metal metabolism in development. The techniques employed are small- and wide-angle x-ray diffraction, x-ray solution scattering and x-ray absorption/emission spectroscopy with micro-beams. The BioCAT facilities provide a resource that is unique on the continent;only SPring-8 in Japan and the ESRF in France provide similar capabilities. Core developments are planned in: 1) Time and spatially resolved Fiber Diffraction for study of muscle, connective tissues, viruses, and structures associated with neurodegerative diseases. 2) Expanded Q-range, high-time resolution and high-throughput small-Angle X-ray Scattering for the study of the low resolution structure of macromolecules in complexes, determination of protein folds in small proteins and domains and time resolved studies of protein and RNA folding. 3) High efficiency microprobe for studies of metal mapping, speciation and local structure as related to cancer, development, and neurodegenerative diseases. Together, these projects will provide both entirely new capabilities and significantly enhanced existing capabilities to our collaborative and service users. Dissemination and training activities will make these capabilities known and available to the wider biomedical community.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR008630-16
Application #
8037732
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Program Officer
Wu, Mary Ann
Project Start
1997-09-30
Project End
2011-12-31
Budget Start
2011-01-01
Budget End
2011-12-31
Support Year
16
Fiscal Year
2011
Total Cost
$1,168,722
Indirect Cost
Name
Illinois Institute of Technology
Department
Other Basic Sciences
Type
Schools of Arts and Sciences
DUNS #
042084434
City
Chicago
State
IL
Country
United States
Zip Code
60616
Orgel, Joseph P R O; Sella, Ido; Madhurapantula, Rama S et al. (2017) Molecular and ultrastructural studies of a fibrillar collagen from octocoral (Cnidaria). J Exp Biol 220:3327-3335
Yazdi, Aliakbar Khalili; Vezina, Grant C; Shilton, Brian H (2017) An alternate mode of oligomerization for E. coli SecA. Sci Rep 7:11747
Sullivan, Brendan; Robison, Gregory; Pushkar, Yulia et al. (2017) Copper accumulation in rodent brain astrocytes: A species difference. J Trace Elem Med Biol 39:6-13
Morris, Martha Clare (2016) Nutrition and risk of dementia: overview and methodological issues. Ann N Y Acad Sci 1367:31-7
Robison, Gregory; Sullivan, Brendan; Cannon, Jason R et al. (2015) Identification of dopaminergic neurons of the substantia nigra pars compacta as a target of manganese accumulation. Metallomics 7:748-55
Gelfand, Paul; Smith, Randy J; Stavitski, Eli et al. (2015) Characterization of Protein Structural Changes in Living Cells Using Time-Lapsed FTIR Imaging. Anal Chem 87:6025-31
Liang, Wenguang G; Ren, Min; Zhao, Fan et al. (2015) Structures of human CCL18, CCL3, and CCL4 reveal molecular determinants for quaternary structures and sensitivity to insulin-degrading enzyme. J Mol Biol 427:1345-1358
Zhou, Hao; Li, Shangyang; Badger, John et al. (2015) Modulation of HIV protease flexibility by the T80N mutation. Proteins 83:1929-39
Baird, Nathan J; Ferré-D'Amaré, Adrian R (2014) Analysis of riboswitch structure and ligand binding using small-angle X-ray scattering (SAXS). Methods Mol Biol 1103:211-25
Nobrega, R Paul; Arora, Karunesh; Kathuria, Sagar V et al. (2014) Modulation of frustration in folding by sequence permutation. Proc Natl Acad Sci U S A 111:10562-7

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