Abstract

Recent studies on the mechanism of protein folding have indicated that proteins can exist as stable intermediate conformers that are structurally and energetically distinct from either native or denatured state. This ability of some proteins to accept an intermediate conformation with unique physical characteristics has an important biological significance, since it is clear that biological function(s) of all proteins are profoundly affected by their structure. Structural and energetical characteristics of human Growth Hormone were studied at pH range from 2.0 to 7.0, in presence or absence of ligands and denaturants. It is known that at low pH hGH has an intermediate state, that makes it to aggregate in solution. We studied this phenomena with the variety of methods, which include ITC, CD, HPLC, etc. Thermodynamic behavior of hGH leads to detailed description of its structural composition and to comprehension on molecular level of its biological role in living systems.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR004328-09
Application #
5224887
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
9
Fiscal Year
1996
Total Cost
Indirect Cost

  Publications

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
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
Lee, R T; Gabius, H J; Lee, Y C (1998) Thermodynamic parameters of the interaction of Urtica dioica agglutinin with N-acetylglucosamine and its oligomers. Glycoconj J 15:649-55
Zakharov, S D; Lindeberg, M; Griko, Y et al. (1998) Membrane-bound state of the colicin E1 channel domain as an extended two-dimensional helical array. Proc Natl Acad Sci U S A 95:4282-7
Luque, I; Todd, M J; Gomez, J et al. (1998) Molecular basis of resistance to HIV-1 protease inhibition: a plausible hypothesis. Biochemistry 37:5791-7
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

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