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Crystal Structure of Hemoglobin from the Maned Wolf (Chrysocyon Brachyurus) Using Synchrotron Radiation

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Crystal structure of hemoglobin isolated from the Brazilian maned wolf (Chrysocyon brachyurus) was determined using standard molecular replacement technique and refined using maximumlikelihood and simulated annealing protocols to 1.87Å resolution. Structural and functional comparisons between hemoglobins from the Chrysocyon brachyurus and Homo sapiens are discussed, in order to provide further insights in the comparative biochemistry of vertebrate hemoglobins.
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Keywords: chrysocyon brachyurus; hemoglobin; maned wolf; synchrotron

Document Type: Review Article

Affiliations: Departamento de Fisica-IBILCE-UNESP. CEP 15054-000. Sao Jose do Rio Preto. SP. Brazil.

Publication date: 2003-12-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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