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Demographic Change And Response: Social Context And The Practice Of Birth Control In Six Countries, Sangeeta Parashar, Harriet B. Presser, Megan L. Klein Hattori, Sara Raley, Zhihong Sa
Demographic Change And Response: Social Context And The Practice Of Birth Control In Six Countries, Sangeeta Parashar, Harriet B. Presser, Megan L. Klein Hattori, Sara Raley, Zhihong Sa
Department of Sociology Faculty Scholarship and Creative Works
This paper expands on Kingsley Davis’s demographic thesis of change and re- sponse. Specifically, we consider the social context that accounts for the primacy of particular birth control methods that bring about fertility change during specific time periods. We examine the relevance of state policy (including national family planning programs), the international population establishment, the medical profession, organized religion, and women’s groups using case studies from Japan, Russia, Puerto Rico, China, India, and Cameroon. Some of these countries are undergoing the second demographic transition, others the first. Despite variations in context, heavy reliance on sterilization and/or abortion as a means …
Desulfovibrio Desulfuricans G20 Tetraheme Cytochrome Structure At 1.5 A˚ And Cytochrome Interaction With Metal Complexes, Mrunalini Pattarkine, J J. Tanner, C A. Bottoms, Y H. Lee, Judy D. Wall
Desulfovibrio Desulfuricans G20 Tetraheme Cytochrome Structure At 1.5 A˚ And Cytochrome Interaction With Metal Complexes, Mrunalini Pattarkine, J J. Tanner, C A. Bottoms, Y H. Lee, Judy D. Wall
Faculty Works
The structure of the type I tetraheme cytochrome c3 from Desulfovibrio desulfuricans G20 was determined to 1.5 A˚ by X-ray crystallography. In addition to the oxidized form, the structure of the molybdate-bound form of the protein was determined from oxidized crystals soaked in sodium molybdate. Only small structural shifts were obtained with metal binding, consistent with the remarkable structural stability of this protein. In vitro experiments with pure cytochrome showed that molybdate could oxidize the reduced cytochrome, although not as rapidly as U(VI) present as uranyl acetate. Alterations in the overall conformation and thermostability of the metal-oxidized protein were investigated …