Findings from University of Essex Update Understanding of Blood Proteins (The Circularly Permuted Globin Domain of Androglobin Exhibits Atypical Heme Stabilization and Nitric Oxide Interaction).

A recent study conducted at the University of Essex in the United Kingdom has provided new insights into the biochemical and structural properties of androglobin, a multi-domain hemoglobin associated with ciliogenesis and spermatogenesis. The researchers used a method for aligning remote homologues, along with molecular modeling and molecular dynamics, to identify a novel structural alignment to other hemoglobins. They found that androglobin exhibits atypical heme stabilization and interacts with nitric oxide, suggesting a potential role in nitric oxide homeostasis or buffering. This study expands our understanding of the functioning of androglobin and its physiological functions. [Extracted from the article]