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Rattlesnake Hemoglobins: Functional Properties and Tetrameric Stability

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The present work analyzed the tetrameric stability of the hemoglobins from the rattlesnake C. durissus terrificus using analytical gel filtration chromatography, SAXS and osmotic stress. We show that the dissociation mechanism proposed for L. miliaris hemoglobin does not apply for these hemoglobins, which constitute stable tetramers even at low concentrations.

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Keywords: Hemoglobin; rattlesnake; tetramer stability

Document Type: Research Article

Affiliations: Depto. de Quimica e Ciencias Ambientais, IBILCE-UNESP, Rua Cristovao Colombo 2265, S.J. do Rio Preto SP, Brazil CEP 15054-000, Brazil.

Publication date: 2006-05-01

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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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