2017/02/28 by Sumith Yesudasan, Xianqiao Wang, Rodney D. Averett
Biochemistry, Genetics and Molecular Biology · Chemistry · Medicine · Physics and Astronomy · #Anisotropy #Biochemistry #Carbon monoxide #Carboxyhemoglobin #Chemistry #Composite material #Computational chemistry #Erythrocyte Function and Pathophysiology #Hemoglobin #Hemoglobin structure and function #Materials science #Molecular dynamics #Optics #Physics #Protein Structure and Dynamics #Shear (geology) #Stiffness #physics.bio-ph
paper · pdf · doi:10.1080/07391102.2017.1323674
published as Journal of Biomolecular Structure and Dynamics, 2017
arxiv created 2017/04/21 · openalex publication_date 2017/04/26 · arxiv updated 2017/05/25 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
We developed a new mechanical model for determining the compression and shear mechanical behavior of four different hemoglobin structures. Previous studies on hemoglobin structures have focused primarily on overall mechanical behavior; however, this study investigates the mechanical behavior of hemoglobin, a major constituent of red blood cells, using steered molecular dynamics (SMD) simulations to obtain anisotropic mechanical behavior under compression and shear loading conditions. Four different configurations of hemoglobin molecules were considered: deoxyhemoglobin (deoxyHb), oxyhemoglobin (HbO2), carboxyhemoglobin (HbCO), and glycated hemoglobin (HbA1C). The SMD simulations were performed on the hemoglobin variants to estimate their unidirectional stiffness and shear stiffness. Although hemoglobin is structurally denoted as a globular protein due to its spherical shape and secondary structure, our simulation results show a significant variation in the mechanical strength in different directions (anisotropy) and also a strength variation among the four different hemoglobin configurations studied. The glycated hemoglobin molecule possesses an overall higher compressive mechanical stiffness and shear stiffness when compared to deoxyhemoglobin, oxyhemoglobin, and carboxyhemoglobin molecules. Further results from the models indicate that the hemoglobin structures studied possess a soft outer shell and a stiff core based on stiffness.