Protein aggregation is associated with various diseases, including Alzheimer and Parkinson
as well as sickle cell disease (SCD). From a molecular point of view, protein aggregation …

The impact upon molecular structure of an additional point mutation adjacent to the existing
E6V mutation in sickle cell hemoglobin was probed spectroscopically. The UV resonance …

Fibers of deoxyhemoglobin S undergo spontaneous crystallization by a mechanism
involving a variety of intermediate structures. These intermediate structures, in common with …

Pathogenesis in sickle cell disease depends on polymerization of deoxyhemoglobin S into
rod-like fibers, forming gels that rigidify red cells and obstruct the systemic microvasculature …

We have characterized new aspects of macrofiber structure and assembly which provide a
mechanism for macrofiber formation from fibers. After the formation of fibers, HbS forms …

Molecular dynamics (MD) simulations have been carried out for 62.5 ps on crystal structures
of deoxy sickle cell hemoglobin (HbS) and normal deoxy hemoglobin (HbA) using the …

We have examined the structure of hemoglobin S fibers, which are associated into large
bundles, or fascicles. Electron micrographs of embedded and cross-sectioned fascicles …

Sickle cell disease is caused by the amino acid substitution of glutamic acid to valine, which
leads to the polymerization of deoxygenated sickle hemoglobin (HbS) into long strands …

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

Sickle cell disease is caused by a point mutation which allows sickle hemoglobin (HbS) to
form long fibers which distort blood cells, impeding circulation. HbS and fetal hemoglobin …