The past decade has been marked by spectacular advances in the areas of genetic engineering, computer technology and in the implementation of sophisticated instrumentation for the study of biological macromolecules. These advances have made possible the development of new approaches to the study of the structure- function relationships in macromolecular systems and particularily in complex assemblies of biological macromolecules like protein- protein, protein-membrane, and protein-DNA complexes to name only three examples. Central to the development of a rigorous, quantitative description of biological structure and function is a knowledge of the forces and the magnitude of the forces involved in the formation of biological structures as well as the energetics of the molecular interactions associated with biological function. The importance of calorimetry, within this context, is that it is the only technique that allows a direct measurement of the magnitude of the forces and energetics associated with biochemical processes. The Biocalorimetry Center at the Johns Hopkins University, the first of its kind in the country, will have a dual commitment. It will provide a user-oriented facility to aid research scientists in the determination of thermodynamic properties of biological systems using state-of-the-art calorimetric instrumentation (high sensitivity differential scanning calorimetry, isothermal reaction calorimetry and multifrequency calorimetry); and, it will focus in the development of new, supersensitive instruments capable of accurately measuring the energetics of biological processes at the subnanomolar level.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
1P41RR004328-01
Application #
3104267
Study Section
(SSS)
Project Start
1988-08-05
Project End
1993-08-04
Budget Start
1988-08-05
Budget End
1989-08-04
Support Year
1
Fiscal Year
1988
Total Cost
Indirect Cost
Name
Johns Hopkins University
Department
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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