Multiscale MD simulations of wild‐type and sickle hemoglobin aggregation
MO Olagunju, J Loschwitz, OO Olubiyi… - Proteins: Structure …, 2022 - Wiley Online Library
Sickle cell disease is a hemoglobinopathy resulting from a point mutation from glutamate to
valine at position six of the β‐globin chains of hemoglobin. This mutation gives rise to …
valine at position six of the β‐globin chains of hemoglobin. This mutation gives rise to …
On the binding free energy and molecular origin of sickle cell hemoglobin aggregation
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 …
as well as sickle cell disease (SCD). From a molecular point of view, protein aggregation …
[PDF][PDF] MULTI-SCALE AND MULTI-PHYSICS MODELING OF SICKLE-CELL DISEASE-PART I MOLECULAR DYNAMICS SIMULATION
Sickle cell anemia is the first disease whose genetic cause was pinpointed at the DNA level
[7]. Sickle cell disease is caused by the switch of a single DNA base pair in the hemoglobin …
[7]. Sickle cell disease is caused by the switch of a single DNA base pair in the hemoglobin …
Molecular dynamics of hemoglobin reveals structural alterations and explains the interactions driving sickle cell fibrillation
In sickle cell anemia, deoxyhemoglobin deforms RBCs by forming fibrils inside that
disintegrate on oxygenation. We studied 100 ns long all-atom molecular dynamics (MD) for …
disintegrate on oxygenation. We studied 100 ns long all-atom molecular dynamics (MD) for …
Effect of T‐R conformational change on sickle‐cell hemoglobin interactions and aggregation
SM Vaiana, MA Rotter, A Emanuele… - Proteins: Structure …, 2005 - Wiley Online Library
We compare the role of a conformational switch and that of a point mutation in the
thermodynamic stability of a protein solution and in the consequent propensity toward …
thermodynamic stability of a protein solution and in the consequent propensity toward …
On the nonaggregation of normal adult hemoglobin and the aggregation of sickle cell hemoglobin
N Galamba - The Journal of Physical Chemistry B, 2019 - ACS Publications
Sickle cell disease is a genetic disorder associated with a single mutation (Glu-β6→ Val-β6)
in the β chains of hemoglobin, causing the polymerization of deoxygenated sickle cell …
in the β chains of hemoglobin, causing the polymerization of deoxygenated sickle cell …
Free energy simulations of axial contacts in sickle‐cell hemoglobin
K Kuczera - Biopolymers, 1996 - Wiley Online Library
Molecular dynamics simulations have been used to investigate the thermodynamic stability
of axial contacts in sickle-cell hemoglobin (HbS). Free energy changes were evaluated for …
of axial contacts in sickle-cell hemoglobin (HbS). Free energy changes were evaluated for …
Modeling of Proteins and Their Interactions with Solvent
Sickle cell anemia is the first disease whose cause was pinpointed at a genetic level.
Hydrophobic interaction is the main cause for sickle hemoglobin (hemoglobin S) sticking to …
Hydrophobic interaction is the main cause for sickle hemoglobin (hemoglobin S) sticking to …
Sickle Cell Hemoglobin Drugged with Cyclic Peptides is Aggregation Incompetent
N Galamba - 2024 - chemrxiv.org
Sickle cell disease is a monogenic blood disorder associated with a mutation in the HBB
gene encoding for the β-globin of normal adult hemoglobin (HbA). This mutation transcribes …
gene encoding for the β-globin of normal adult hemoglobin (HbA). This mutation transcribes …
The role of pH on instability and aggregation of sickle hemoglobin solutions
M Manno, PL San Biagio… - … : Structure, Function, and …, 2004 - Wiley Online Library
Understanding the physical basis of protein aggregation covers strong physical and
biomedical interests. Sickle hemoglobin (HbS) is a point‐mutant form of normal human adult …
biomedical interests. Sickle hemoglobin (HbS) is a point‐mutant form of normal human adult …