The Biocalorimetry Center is the only center of its kind in the United States. It is dedicated to the development of new calorimetric technologies and the application of those technologies in Biomedical Research. It also plays an important role in the training of scientists in the area of calorimetry and in the dissemination of the capabilities of these technologies within the scientific community. Calorimetry is the only technique with the ability to measure the energetics of chemical or biochemical reactions. Since the folding of proteins into their native structures, the degree of advancement of biochemical reactions, the association of biological molecules, the binding of ligands or pathogens to cells or the formation of biological structures in general are dictated by their energetics, calorimetry plays a fundamental role in the development of a complete understanding of these processes and the ability to engineer or modify them. During the last five years, significant advances have been made in these technologies as reflected by the fact that many biological reactions can now be measured using microgram amounts of material. Also, during the last five years, significant advances have been made in the development of new methods of analysis, particularly in the area of Structural Thermodynamics. Continuous developments in this area will bring about the capability to accurately predict the stability of proteins from structural parameters or to predict the binding ability of peptide hormones or other molecules to protein receptors. For the next funding period the development of a new generation of highly sensitive calorimeters is planned. These instruments include a differential scanning calorimeter, multifrequency calorimeter, isothermal titration calorimeter, flow/mix calorimeter and a discrete flow/variable temperature calorimeter. A major effort will be made in the area of Structural Thermodynamics and in the development of a Protein Thermodynamics Database. Also the Biocalorimetry Center is engaged in many collaborative projects with scientists from many laboratories around the country.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR004328-10
Application #
2520036
Study Section
Special Emphasis Panel (SSS (P1))
Project Start
1988-08-05
Project End
1998-08-04
Budget Start
1997-08-05
Budget End
1998-08-04
Support Year
10
Fiscal Year
1997
Total Cost
Indirect Cost
Name
Johns Hopkins University
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
045911138
City
Baltimore
State
MD
Country
United States
Zip Code
21218
Jaganaman, Sunil; Pinto, Alex; Tarasev, Michael et al. (2007) High levels of expression of the iron-sulfur proteins phthalate dioxygenase and phthalate dioxygenase reductase in Escherichia coli. Protein Expr Purif 52:273-9
Todd, M J; Gomez, J (2001) Enzyme kinetics determined using calorimetry: a general assay for enzyme activity? Anal Biochem 296:179-87
Karantza, V; Freire, E; Moudrianakis, E N (2001) Thermodynamic studies of the core histones: stability of the octamer subunits is not altered by removal of their terminal domains. Biochemistry 40:13114-23
Griko, Y V; Remeta, D P (1999) Energetics of solvent and ligand-induced conformational changes in alpha-lactalbumin. Protein Sci 8:554-61
Chu, V; Freitag, S; Le Trong, I et al. (1998) Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system. Protein Sci 7:848-59
Luque, I; Freire, E (1998) Structure-based prediction of binding affinities and molecular design of peptide ligands. Methods Enzymol 295:100-27
Luque, I; Gomez, J; Semo, N et al. (1998) Structure-based thermodynamic design of peptide ligands: application to peptide inhibitors of the aspartic protease endothiapepsin. Proteins 30:74-85
Gomez, J; Semo, N; Freire, E (1998) Structural thermodynamic study of the binding of renin inhibitors to endothiapepsin. Adv Exp Med Biol 436:325-8
Koder, R L; Miller, A F (1998) Overexpression, isotopic labeling, and spectral characterization of Enterobacter cloacae nitroreductase. Protein Expr Purif 13:53-60
Freire, E (1998) Statistical thermodynamic linkage between conformational and binding equilibria. Adv Protein Chem 51:255-79

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