Functional roles of the heme architecture and its environment in tetraheme cytochrome c

Article Abstract:

The mutliheme structure of the c-type tetraheme cytochromes have hemes covalently bonded to polypeptides, where each heme behaves like a domain. The tetraheme cytochromes c are not just simple heme assemblies but sophisticated mechanisms that regulate the extremely low redox potentials of the cytochrome [c.sub.3], bis-imidazole coordination and heme exposure through their chain-like architecture.

Analysis, Nuclear magnetic resonance spectroscopy, Oxidation-reduction reaction, Oxidation-reduction reactions, Cytochrome c, Chemical properties

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Structural genomics of membrane proteins

Article Abstract:

This article discusses a collaborative facility set-up in Japan for conducting genomics research on membrane proteins. The project envisages developing methodologies for protein structural studies and ligand-receptor interaction employing electron microscopy, X-ray crystallography, nuclear magnetic resonance spectroscopy, and computer simulation.

Japan, Methods, Membrane proteins, Simulation methods, Simulation, X-ray crystallography

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The Southeast Collaboratory for Structural Genomics: a high-throughput gene to structure factory

Article Abstract:

This article describes the structural organization and research collaboration activities of the Southeast Collaboratory for Structural Genomics. The facility composed of five academic partner institutions in the southeast share individual and defined area of work in the overall scheme of gene to protein structure project.

United States, Management dynamics, Management, Proteins, Crystallography, Company business management, Action research

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