Water, ions, and hemoglobin: effects on allostery and polymerization
MA Rotter, J Jiang, SM Ferrone… - The Journal of Physical …, 2018 - ACS Publications
Proteins that function in aqueous solution can be perturbed by the solvent. Here we present
experimental studies on two such interactions in the hemoglobin molecule.(1) Hemoglobin's …
experimental studies on two such interactions in the hemoglobin molecule.(1) Hemoglobin's …
Crowding and the polymerization of sickle hemoglobin
FA Ferrone, MA Rotter - Journal of Molecular Recognition, 2004 - Wiley Online Library
Under physiological conditions, sickle hemoglobin, a natural mutant of human hemoglobin A
with a surface hydrophobic valine in place of a negatively charged glutamic acid …
with a surface hydrophobic valine in place of a negatively charged glutamic acid …
Flexibility and nucleation in sickle hemoglobin
M Ivanova, R Jasuja, L Krasnosselskaia… - Journal of molecular …, 2001 - Elsevier
We have studied the self-assembly of Hemoglobin C-Harlem (HbC-Harlem), a double
mutant of hemoglobin that possesses the β6 Glu→ Val mutation of sickle hemoglobin (HbS) …
mutant of hemoglobin that possesses the β6 Glu→ Val mutation of sickle hemoglobin (HbS) …
Ligand binding and the gelation of sickle cell hemoglobin
J Hofrichter - Journal of Molecular Biology, 1979 - Elsevier
The solubility equilibrium between monomer and polymer which has been shown to exist in
deoxyhemoglobin S solutions is examined in solutions partially saturated with carbon …
deoxyhemoglobin S solutions is examined in solutions partially saturated with carbon …
Universal metastability of sickle hemoglobin polymerization
W Weng, A Aprelev, RW Briehl, FA Ferrone - Journal of molecular biology, 2008 - Elsevier
Sickle hemoglobin (HbS) polymerization occurs when the concentration of deoxyHbS
exceeds a well-defined solubility. In experiments using sickle hemoglobin droplets …
exceeds a well-defined solubility. In experiments using sickle hemoglobin droplets …
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 …
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 of sickle hemoglobin polymerization: a scaled-particle treatment for use with dextran as a crowding agent
Z Liu, W Weng, RM Bookchin, VL Lew, FA Ferrone - Biophysical journal, 2008 - cell.com
Fundamental to the analysis of protein polymerization is the free energy of association,
typically determined from solubility. It has been previously shown that concentrated 70kDa …
typically determined from solubility. It has been previously shown that concentrated 70kDa …
Interpretation of the osmotic behavior of sickle cell hemoglobin solutions: different interactions among monomers and polymers
J Han, J Herzfeld - Biopolymers: Original Research on …, 1998 - Wiley Online Library
It has long been known that a simple hard particle model quantitatively explains the osmotic
properties of monomeric hemoglobin near its isoelectric point. However, we find that a hard …
properties of monomeric hemoglobin near its isoelectric point. However, we find that a hard …
Nucleation and polymerization of sickle hemoglobin with Leu β88 substituted by Ala
Z Cao, D Liao, R Mirchev, JJM de Llano… - Journal of molecular …, 1997 - Elsevier
We have measured the solubility, and the rates of homogeneous and heterogeneous
nucleation on sickle hemoglobin (HbSβ6 Glu→ Val) additionally modified by site-directed …
nucleation on sickle hemoglobin (HbSβ6 Glu→ Val) additionally modified by site-directed …