Continued progress in biomedical research requires the determination of structures not just of individual molecules but of macromolecular assemblies such as those that mediate essential cellular processes like transcription and replication. Synchrotron crystallography using an undulator source is a powerful tool with which to analyze the structure of assemblies with their large size and complexity. Understanding the dynamics of large assemblies and their intra-molecular rearrangements is a challenging problem. Time-resolved synchrotron x-ray footprinting is an ideal method for gaining insight into these important processes. Structural examination of macromolecules, cells, and tissues using microscopy techniques can be significantly enhanced with synchrotron infrared microspectroscopy. Both the far-and mid-infrared regions can be used to examine protein folding and dynamics, while microscopy, utilize to examine cells and tissues, provides chemically specific information about the biological processes under study. The Albert Einstein Center for Synchrotron Biosciences, with facilities and laboratories at the National Synchrotron Light Source and the Albert Einstein College of Medicine, is developing new biomedical technologies as core research projects in each of the three areas highlighted above. The core research is driven by twenty-one collaborative projects from the laboratories of well-funded investigators expert in the various research areas. The service function of the Resource Center also provide invaluable access to synchrotron light for macromolecular crystallography, EXAFS, and small-angle scattering studies of numerous NIH funded laboratories. Many of the biologically focused collaborative and service projects are impacted by more than one core technological activity. These inter- relationships give rise to significant synergy in the Resource Center's activities, particularly for projects involving macromolecular folding, transcriptional control, signal transduction, and polymerase function. Since the funding of the Resource Center two years ago, numerous faculty, staff, and students from the College of Medicine and from our fellow academic institutions in the New York Metropolitan area have become actively involved in these research activities. The Resource Center has become an important part of the College of Medicine's overall Biomedical Research Mission and is an important regional focus for biomedical research as well as an established national and international presence in synchrotron bioscience.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-17
Application #
6056680
Study Section
Special Emphasis Panel (ZRG3-SSS-6 (03))
Program Officer
Swain, Amy L
Project Start
1982-08-01
Project End
2003-08-31
Budget Start
1999-09-01
Budget End
2000-08-31
Support Year
17
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Albert Einstein College of Medicine
Department
Physiology
Type
Schools of Medicine
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461
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Masip, Lluis; Pan, Jonathan L; Haldar, Suranjana et al. (2004) An engineered pathway for the formation of protein disulfide bonds. Science 303:1185-9
Huang, Raymond Y; Miller, Lisa M; Carlson, Cathy S et al. (2003) In situ chemistry of osteoporosis revealed by synchrotron infrared microspectroscopy. Bone 33:514-21
Rashidzadeh, Hassan; Khrapunov, Sergei; Chance, Mark R et al. (2003) Solution structure and interdomain interactions of the Saccharomyces cerevisiae ""TATA binding protein"" (TBP) probed by radiolytic protein footprinting. Biochemistry 42:3655-65
Uchida, Takeshi; Takamoto, Keiji; He, Qin et al. (2003) Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme. J Mol Biol 328:463-78
Taylor, Colleen M; Watton, Stephen P; Bryngelson, Peter A et al. (2003) Inner-sphere complexation of cobalt(II) 2,9-dimethyl-1,10-phenanthroline ([Co(neo)]2+) with commercial and sol-gel derived silica gel surfaces. Inorg Chem 42:312-20
Dewan, John C; Feeling-Taylor, Angela; Puius, Yoram A et al. (2002) Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution. Acta Crystallogr D Biol Crystallogr 58:2038-42
Kiselar, J G; Maleknia, S D; Sullivan, M et al. (2002) Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry. Int J Radiat Biol 78:101-14
Swisher, Jennifer F; Su, Linhui J; Brenowitz, Michael et al. (2002) Productive folding to the native state by a group II intron ribozyme. J Mol Biol 315:297-310
Dhavan, Gauri M; Crothers, Donald M; Chance, Mark R et al. (2002) Concerted binding and bending of DNA by Escherichia coli integration host factor. J Mol Biol 315:1027-37

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