Multivalent interactions between receptors and glycans play an important role in many
different biological processes, including pathogen infection, self-recognition, and the …

This mini-review, mainly based on our resonance Raman studies on the structural origin of
cooperative O2 binding in human adult hemoglobin (HbA), aims to answering why HbA is a …

The study of hemoglobin oxygenation, starting from the classical works of Hill, has laid the
foundation for molecular biophysics. The cooperative nature of oxygen binding to …

Background. Community consumption of herbal plants in developing countries is a common
practice, however, scarcity of information on their physiochemical composition is a major …

Hemoglobin (Hb) is well protected inside the red blood cells (RBCs). Upon hemolysis and
when free in circulation, Hb can be involved in a range of radical generating reactions and …

A heme oxygen binding behavior was described through a unique geometric and electronic
comparison of zinc porphyrin complexes. In this work, a charge transfer model for saddled …

Despite the fact that the investigation of the structural and functional properties of
hemoglobin dates back more than 150 years, the topic has not lost its relevance today. The …

Hemoglobin and red blood cells (erythrocytes) have been studied extensively from the
perspective of life and biomedical sciences. However, no analysis of hemoglobin and red …

Sickle cell disease (SCD) is a structural and monogenetic genetic disorder due to a mutation
that occurs in the globin β-chain, resulting in the formation of hemoglobin S (Hb S), a protein …

Using various mutants, we investigated to date the roles of the Fe-histidine (F8) bonds in
cooperative O 2 binding of human hemoglobin (Hb) and differences in roles between α-and …