This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.The design and development of the Cryogenic FTMS, as a collaborative project with the Cardiovascular Proteomics Center, is a major project at the moment. The instrument is currently under construction and awaiting the magnet which should be delivered in the summer of 2005.Fourier Transform Mass Spectrometry is limited in its base performance characteristics (resolution, sensitivity, mass accuracy, et cetera) by three fundamental instrumental limitations, pressure, magnetic-field strength, and preamplifier noise. The need for low pressure implies need for a large bore for large conductance to the pumps, but the need for high field with high homogeneity implies the need for low bore diameter to simplify magnet design. Designing an FTMS for operation in the cold bore of a superconducting magnet eliminates this contradiction as the bore itself becomes a cryopump. Because the cold bore acts as a cryopump, the ion transfer vacuum chamber can be made substantially narrower than normal, allowing use of narrower bore magnets than are normally used in FTMS while still achieving the needed 60W at 50K. Due to the narrower 3? bore, the magnet has been designed as a 15 Tesla magnet which will achieve acceptance specifications at 14 Tesla. The bore is designed with two copper mounting brackets which will function as thermal anchors for the inner FTMS vacuum chamber. However, due to the large surface areas involved, the primary heat transfer will be due to direct radial radiative heat transfer, which will allow most of the heat flowing down the vacuum chamber walls to be transferred to the 50K shield before it reaches the 4K region. Thermal analysis shows that it is possible to build a vacuum chamber which can transmit less than 0.5W of heat from the source to the cell. The instrument is now under construction, and installation of the magnet id pending. The magnet has met field (14T) and homogeneity specifications (10 ppm over a 40 mm long by 40 mm diameter cylinder) and is currently being vacuum tested in the final dewar.The magnet was installed at BUSM and met field at 14T, and the ion source is assembled. The FTMS insert was assembled, and initial data is available and submitted for publication. Currently, the system is being upgraded with the low noise preamplifier and alignment, centering, and electrical connections at the ICR cell are being improved.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR010888-12
Application #
7722972
Study Section
Special Emphasis Panel (ZRG1-BCMB-H (40))
Project Start
2008-06-01
Project End
2009-05-31
Budget Start
2008-06-01
Budget End
2009-05-31
Support Year
12
Fiscal Year
2008
Total Cost
$7,774
Indirect Cost
Name
Boston University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
604483045
City
Boston
State
MA
Country
United States
Zip Code
02118
Lu, Yanyan; Jiang, Yan; Prokaeva, Tatiana et al. (2017) Oxidative Post-Translational Modifications of an Amyloidogenic Immunoglobulin Light Chain Protein. Int J Mass Spectrom 416:71-79
Sethi, Manveen K; Zaia, Joseph (2017) Extracellular matrix proteomics in schizophrenia and Alzheimer's disease. Anal Bioanal Chem 409:379-394
Hu, Han; Khatri, Kshitij; Zaia, Joseph (2017) Algorithms and design strategies towards automated glycoproteomics analysis. Mass Spectrom Rev 36:475-498
Ji, Yuhuan; Bachschmid, Markus M; Costello, Catherine E et al. (2016) S- to N-Palmitoyl Transfer During Proteomic Sample Preparation. J Am Soc Mass Spectrom 27:677-85
Hu, Han; Khatri, Kshitij; Klein, Joshua et al. (2016) A review of methods for interpretation of glycopeptide tandem mass spectral data. Glycoconj J 33:285-96
Pu, Yi; Ridgeway, Mark E; Glaskin, Rebecca S et al. (2016) Separation and Identification of Isomeric Glycans by Selected Accumulation-Trapped Ion Mobility Spectrometry-Electron Activated Dissociation Tandem Mass Spectrometry. Anal Chem 88:3440-3
Wang, Yun Hwa Walter; Meyer, Rosana D; Bondzie, Philip A et al. (2016) IGPR-1 Is Required for Endothelial Cell-Cell Adhesion and Barrier Function. J Mol Biol 428:5019-5033
Steinhorn, Benjamin S; Loscalzo, Joseph; Michel, Thomas (2015) Nitroglycerin and Nitric Oxide--A Rondo of Themes in Cardiovascular Therapeutics. N Engl J Med 373:277-80
Walsh, Erica M; Niu, MengMeng; Bergholz, Johann et al. (2015) Nutlin-3 down-regulates retinoblastoma protein expression and inhibits muscle cell differentiation. Biochem Biophys Res Commun 461:293-9
Théberge, Roger; Dikler, Sergei; Heckendorf, Christian et al. (2015) MALDI-ISD Mass Spectrometry Analysis of Hemoglobin Variants: a Top-Down Approach to the Characterization of Hemoglobinopathies. J Am Soc Mass Spectrom 26:1299-310

Showing the most recent 10 out of 253 publications