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The focus of this research was the characterization of three metallroteins. The characterization was based on the information obtained from their structures and biochemical data obtained from in-vitro and in-vivo experiments. The structures of the three proteins studied were obtained by x-ray crystallography. The first protein studied was the hemerythrin-like domain from the Desulfovibrio vulgaris chemoreceptor H, DcrH-Hr. The second protein was the Bacillus subtilis M32 carboxypeptidase, BsuCP. And the third protein was one of the M32 carboxypeptidases from Leishmania major, LmaCP.

Produktbeschreibung
The focus of this research was the characterization of three metallroteins. The characterization was based on the information obtained from their structures and biochemical data obtained from in-vitro and in-vivo experiments. The structures of the three proteins studied were obtained by x-ray crystallography. The first protein studied was the hemerythrin-like domain from the Desulfovibrio vulgaris chemoreceptor H, DcrH-Hr. The second protein was the Bacillus subtilis M32 carboxypeptidase, BsuCP. And the third protein was one of the M32 carboxypeptidases from Leishmania major, LmaCP.
Autorenporträt
Clara E. Isaza has been an Assistant Professor at Universidad Autónoma de Nuevo León (México) since 2006; currently she is also collaborating with the Industrial Engineering Department at Universidad de Puerto Rico (Mayaguez). Professor Michael Chan of The Ohio State University (USA) is affiliated to the Biochemistry and Chemistry Departments.