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当前位置: 香港环球分析 > 最新动态 > 2006等温滴定微量热仪(ITC)交流会应用专家简介

2006等温滴定微量热仪(ITC)交流会应用专家简介

香港环球分析

2006/11/29 10:22

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Christin T. Choma
Senior Biophysicist


EDUCATION/TRAINING  
Carleton University, Ottawa B.Sc. 1973-1980 Biology
Carleton University, Ottawa M.Sc. 1980-1982 Biology
University of Ottawa, Ottawa Ph.D. 1987-1991 Biochemistry
National Research Council, Ottawa Postdoc 1990-1991 Spectroscopy
DuPont, Wilmington, Delaware Postdoc 1991-1994 Protein Design
NOTE: The Biographical Sketch may not exceed four pages. Items A and B (together) may not exceed two of the four-page limit.  Follow the formats and instructions on the attached sample.


A. Positions and Honors. List in chronological order previous positions, concluding with your present position. List any honors. Include present membership on any Federal Government public advisory committee.


1983-1984: Research Assistant, Queens University, Kingston, Canada
1984-1985: Research Assistant, Allelix Inc., Toronto
1985-1990: Staff Scientist, Canadian Astronautics Ltd., Ottawa
1994-1998: Principal Scientist, Protein Engineering Facility, Groningen, The Netherlands
1998-1999: Associate Director, Johnson Research Foundation, University of Pennsylvania, Philadelphia
1999-2005: Associate Professor, tenure-track, Rensselaer Polytechnic Institute, Troy, NY
2006-present: Senior Biophysicist, Calorimetry Sciences Corp., Lindon, UT


Awards: National Sciences and Engineering Research Council of Canada Postdoctoral Fellowship, 1991-1993




B. Selected peer-reviewed publications (in chronological order). Do not include publications submitted or in preparation.


Choma, C. T., K. Kaestle, K. Akerfeldt, R. Kim, J. Groves and W. DeGrado (1994). A general method for coupling unprotected peptides to bromoacetamido porphyrin templates. Tetrahedron Lett. 34, 6191-6194.


Choma, C.T., J. Lear, M. Nelson, D. Robertson, L. Dutton and W.F. DeGrado (1994).  Design of a heme-binding four-helix bundle. J. Am. Chem. Soc. 116, 856-865.


Englebretsen, D.R., C.T. Choma and G.T. Robillard (1998). Synthesis of a designed transmembrane protein by thioether ligation of solubilised segments: N-haloacetylated peptides survived resin cleavage using TFA and EDT as scavenger. Tetrahedron Lett. 39, 4929-4932.


Choma, C.T., G.T. Robillard and D.R. Englebretsen (1998). Synthesis of hydrophobic peptides: an Fmoc ‘solubilizing tail’ method. Tetrahedron Lett. 39, 2417-2420.


Choma, C.T., E. Schudde, R. Kellogg, G.T. Robillard and B.L. Feringa (1998). A functional mimic of natural peroxidases: synthesis and catalytic activity of a non-heme iron/peptide hydroperoxide complex. J. Chem. Soc., Perkin Trans. 1, 1998, 769-773.


Choma, C.T., H. Gratkowski, J. Lear, W.F. DeGrado. (2000) Asparagine-mediated self-assembly of a model transmembrane helix. Nature Structural Biology 7, 161-166.


Choma, C.T., D.P. Tieleman, D. Cregut, L. Serrano and H.J.C. Berendsen. (2001) Towards the design and computational characterization of a membrane protein. J. Mol. Graph. Mod. 20, 219-234.


Stewart, N. A., V. T. Pham, C. T. Choma and H. Kaplan. (2002) Improved peptide detection with matrix-assisted laser desorption/adsorption mass spectrometry by trimethylation of amino groups. Rapid Commun. Mass Spectrom. 16 1448-1453.


Van den Heuvel, M., T. van den Berg, R. Kellogg, C.T. Choma and B. Feringa. (2004) Synthesis of a non-heme template for attaching four peptides: an approach to artificial iron(II)-containing peroxidases. J. Org. Chem. 69 250-262.


Laremore, T. N., D. M. Weber and C. T. Choma. (2005) An evaluation of the utility of in vacuo methylation for mass-spectrometry-based analyses of peptides. Rapid Commun. Mass Spectrom. 19 2045-2054.


Kojima, T., D. M. Weber and C. T. Choma. (2005) {N-[Bis(2-pyridyl)methyl]-N,N-bis(2-pyridylmethyl)amine-5N}chlororuthenium(II) perchlorate methanol solvate. Acta Cryst. E61, m226-m228.


Kojima, T., D. M. Weber and C. T. Choma. (2005) {N-[Bis(2-pyridyl)methyl]-N,N-bis(2-pyridyl)methylamine-5N}chlorozinc(II) perchlorate monohydrate. Acta Cryst. E60, m1291-m1292.


C.  Research Support. List selected ongoing or completed (during the last three years) research projects (federal and non-federal support). Begin with the projects that are most relevant to the research proposed in this application. Briefly indicate the overall goals of the projects and your role (e.g. PI, Co-Investigator, Consultant) in the research project. Do not list award amounts or percent effort in projects.


Research terminated upon leaving academia 12/05


Petroleum Research Fund 40302-AC4 Choma (PI) 1/2004-8/2006
The Design of Synthetic Catalytic Cofactor-Protein Complexes Funds were used primarily to investigate Ruthenium-mediated catalysis in synthetic cofactors.


Rensselaer Polytechnic Institute H71086 Choma (PI) 4/2001-
A novel technique for the facile identification of expressed proteins in cells Funds were used to initiate in vacuo research into protein trimethylation.


Completed Research


Foundation for Chemical Research in the Netherlands Choma (PI) 11/1997-10/2001
Enzymes and enzyme models Funds were used to support a doctoral student working on the synthesis of novel chemical catalysts for incorporation into designed proteins.


Japan Society for the Promotion of Science Choma (PI) 4/2002-3/2003
Investigation of the Catalytic Activity of Ruthenium and Zinc Complexes of the N4Py Ligand
This grant provided support for a two-month sabbatical in Japan, combining a lecture tour and research at the University of Kyushu.


Howard Hughes Medical Institute Choma (Co-PI) 9/2002-8/2003
Undergraduate Science Education Program
This grant was used to design two new laboratory courses in proteomics research at the undergraduate and graduate level.


National Science Foundation CHE-0078056 Choma (Co-PI) 9/2000-8/2004
Acquisition of a MALDI-TOF Mass Spectrometer Funds were used to purchase the TofSpec 2E MALDI-TOF mass spectrometer which featured prominently in my research.


Research Corporation R10684 Choma (PI) 1/2001-12/2005
De Novo Design Of A Functional Mimic Of A Natural Enzyme
This grant looked at the design of hydrophobic binding pockets in four-helix bundle proteins.

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