The Resource center based on the facilities of beamline X-9B at the National Synchrotron Light Source (NSLS) has been at the forefront of using x-ray absorption spectroscopy (XAS) to address critical questions of biological structure. The proposal outlines plans to focus the efforts of the X-9B resource on s Regional Center for Time Resolved Synchrotron Spectroscopy that can provide core, collaborative, service, training, and dissemination functions in order that important problems in biological dynamics can be immediately addressed. This center will be based on facilities available at NSLS beamline X-9B the U12 infrared line and in several white radiation lines. An accompanying spectroscopy laboratory at NSLS, the investigator's spectroscopy and biochemistry laboratory facilities at the Albert Einstein College of Medicine and the laboratory of Dr. Michael Brenowitz both located at AECOM will also be available. Time resolved methods of structural spectroscopy have been particularly valuable in investigating the dynamics of key structures for a variety of proteins. This proposal has as its focus instrument developments and related collaborative projects that probe these dynamic changes using XAS time resolved x-ray footprinting and time resolved IR spectroscopy. The core instrumentation development focuses on freeze quench and flow devices for XAS to access the structure of intermediate states on millisecond timescales; optical pump, x-ray probe methods to provide structural information on submicrosecond to millisecond timescales, and related developments in data analysis and spectroscopic monitoring, to provide for appropriate analytical methods and assurance of sample integrity. Methods for time resolved x-ray foot printing and time resolved IR spectroscopy will also be developed.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001633-13A2
Application #
2281551
Study Section
Special Emphasis Panel (ZRG7-SSS-W (03))
Project Start
1982-08-01
Project End
1998-09-29
Budget Start
1995-09-30
Budget End
1996-09-29
Support Year
13
Fiscal Year
1995
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
Vongsvivut, Jitraporn; Fernandez, Jason; Ekgasit, Sanong et al. (2004) Characterization of supported cylinder-planar germanium waveguide sensors with synchrotron infrared radiation. Appl Spectrosc 58:143-51
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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