Solution studies on heme proteins circular dichroism and optical rotation of Glycera dibranchiata hemoglobins
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference48 articles.
1. The function of coelomic cell hemoglobin in the polychaete Glycera dibranchiata
2. The Intracellular Hemoglobins of a Polychaete
3. Heterogeneity of the Hemoglobin from the Common Bloodworm Glycera dibranchiata
4. Physicochemical Properties of the Hemoglobins from the Common Bloodworm Glycera dibranchiata
5. The haemoglobin systems of the bloodworms Glycera dibranchiata and G. americana. Oxygen binding properties of haemolysates and component haemoglobins
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1. Structural Insights into the Heme Pocket and Oligomeric State of Non-Symbiotic Hemoglobins from Arabidopsis thaliana;Biomolecules;2020-11-29
2. Circular dichroism spectroscopy ofLucina Ihemoglobin;FEBS Letters;1997-07-14
3. Properties of a recombinant human hemoglobin with aspartic acid 99 (β), an important intersubunit contact site, substituted by lysine;Protein Science;1994-08
4. [13] Stationary and time-resolved circular dichroism of hemoglobins;Methods in Enzymology;1994
5. CD studies on the reversed heme orientation in monomeric Glycera dibranchiata hemoglobins;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1988-01
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