Abstract

Structural and functional properties will be examined for several proteins of physiological interest: hemoglobin, cytochromes, calcium binding protein, and polypeptide hormones such as human chorionic somatomammotropin and its pituitary analogs growth hormone and prolactin. Biophysical and biochemical techniques to be employed include macromolecular X-ray crystallography, stopped-flow flash photolysis kinetics, fluorescence, and both EXAFS and diffraction techniques which exploit the unique properties of synchrotron radiation. For each protein, we are interested in those aspects of its structure which are particularly related to its physiological function. Thus for hemoglobin and cytochromes, we concentrate on the heme group and its interaction with the surrounding protein; for calcium binding protein, on its interaction with calcium and other ions; and for the hormones, on their overall structure. Hemoglobin is involved in respiration, the transport of oxygen and carbon dioxide between the lungs and the tissues; cytochromes, in electron transport and cellular energy production; calcium binding protein, in intestinal absorption and translocation of calcium; and hormones such as human chorionic somatomammotropin, growth hormone and prolactin, in growth-promoting and lactogenic activities.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM029044-05
Application #
3276503
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1981-05-01
Project End
1986-04-30
Budget Start
1985-05-01
Budget End
1986-04-30
Support Year
5
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Cornell University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Ithaca
State
NY
Country
United States
Zip Code
14850

  Publications

Caffrey, M (1989) A lyotrope gradient method for liquid crystal temperature-composition-mesomorph diagram construction using time-resolved x-ray diffraction. Biophys J 55:47-52
Moffat, K; Bilderback, D; Schildkamp, W et al. (1989) Laue photography from protein crystals. Basic Life Sci 51:325-30
Moffat, K (1989) Time-resolved macromolecular crystallography. Annu Rev Biophys Biophys Chem 18:309-32
Szebenyi, D M; Moffat, K (1987) Determination of the three-dimensional structure of vitamin D-dependent calcium-binding protein from bovine intestine. Methods Enzymol 139:585-610
Caffrey, M (1987) Kinetics and mechanism of transitions involving the lamellar, cubic, inverted hexagonal, and fluid isotropic phases of hydrated monoacylglycerides monitored by time-resolved X-ray diffraction. Biochemistry 26:6349-63
Caffrey, M; Hing, F S (1987) A temperature gradient method for lipid phase diagram construction using time-resolved x-ray diffraction. Biophys J 51:37-46
Caffrey, M; Werner, B G; Priestley, D A (1987) A crystalline lipid phase in a dry biological system: evidence from X-ray diffraction analysis of Typha latifolia pollen. Biochim Biophys Acta 921:124-34
Spitsberg, V L (1987) A selective extraction of growth hormone from bovine pituitary gland and its further purification and crystallization. Anal Biochem 160:489-95
Szebenyi, D M; Moffat, K (1986) The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins. J Biol Chem 261:8761-77
Simolo, K; Korszun, Z R; Stucky, G et al. (1986) Extended X-ray absorption fine structure studies of Zn2Fe2 hybrid hemoglobins: absence of heme bond length changes in half-ligated species. Biochemistry 25:3773-8

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