We have measured homogeneous and heterogeneous nucleation rates of sickle
hemoglobin (HbS) in the presence of a strongly binding deletion mutant of the cytoplasmic …

A recent molecular dynamics investigation into the stability of hemoglobin concluded that the
unliganded protein is only stable in the T state when a solvent box is used in the simulations …

Many proteins contain cofactors, such as heme, ATP and metal ions. Binding of cofactors is
not only essential for their biological functions, but also can reshape the intrinsic energy …

A mutation at the sixth residue, glutamic acid to valine, in beta chain of hemoglobin distorts
the entire shape of hemoglobin into a sickle shape. The investigation of the binding …

Increasing the affinity of hemoglobin for oxygen represents a feasible and promising
therapeutic approach for sickle cell disease by mitigating the primary pathophysiological …

Sickle hemoglobin (HbS) is a point mutation of the two β subunits in normal Hb (HbA) that
leads to nucleated polymerization and accompanying pathology. We measured the rates of …

We probe the role of free heme in the interactions between sickle cell hemoglobin (HbS)
molecules in simulated physiological solutions: polymerization of deoxy‐HbS is the primary …

Freezing of protein solutions is required for many applications such as storage, transport, or
lyophilization; however, freezing has inherent risks for protein integrity. It is difficult to study …

Atomistic molecular dynamics simulations of human serum albumin in the presence and
absence of disulfide bonds are presented. Simulations of 70 ns duration provide information …

Aggregation of proteins is an undesired phenomena that affects both human health and
bioengineered products such as therapeutic proteins. Finding preventative measures could …