Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
5R01NS024520-10
Application #
2265266
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1986-07-01
Project End
1997-02-28
Budget Start
1995-03-01
Budget End
1997-02-28
Support Year
10
Fiscal Year
1995
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
Johnson, C R; Angeletti, M; Pucciarelli, S et al. (1996) Oxygen binding to fallow-deer (Dama dama) hemoglobin: stepwise enthalpies at pH 7.4. Biophys Chem 59:107-17
Hilser, V J; Freire, E (1995) Quantitative analysis of conformational equilibrium using capillary electrophoresis: applications to protein folding. Anal Biochem 224:465-85
Freire, E (1995) Thermal denaturation methods in the study of protein folding. Methods Enzymol 259:144-68
Murphy, K P; Freire, E (1995) Thermodynamic strategies for rational protein and drug design. Pharm Biotechnol 7:219-41
Gomez, J; Hilser, V J; Xie, D et al. (1995) The heat capacity of proteins. Proteins 22:404-12
Murphy, K P; Freire, E; Paterson, Y (1995) Configurational effects in antibody-antigen interactions studied by microcalorimetry. Proteins 21:83-90
Johnson, C R; Morin, P E; Arrowsmith, C H et al. (1995) Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor. Biochemistry 34:5309-16
Freire, E (1995) Differential scanning calorimetry. Methods Mol Biol 40:191-218
Gomez, J; Freire, E (1995) Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J Mol Biol 252:337-50
Freire, E (1995) Thermodynamics of partly folded intermediates in proteins. Annu Rev Biophys Biomol Struct 24:141-65

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