Results 71 to 80 of about 20,301,451 (210)
Hemoglobin Strain Field Waves and Allometric Functionality [PDF]
arXiv, 2016 Hemoglobin (Hgb) forms tetramers (dimerized dimers), which enhance its globular stability and may also facilitate small gas molecule transport, as shown by recent all-atom Newtonian solvated simulations. Hydropathic bioinformatic scaling reveals many wave-like features of strained Hgb structures at the coarse-grained amino acid level, while ...
arxiv
Genetic and clinical features of hemoglobin H disease in Chinese patients.
New England Journal of Medicine, 2000 BACKGROUND Normally, one pair of each of the two alpha-globin genes, alpha1 and alpha2, resides on each copy of chromosome 16. In hemoglobin H disease, three of these four alpha-globin genes are affected by a deletion, a mutation, or both. We studied the
Frederick E. Chen +7 more
semanticscholar +1 more source
Structural interpretation of the amino acid sequence of a second domain from the Artemia covalent polymer globin [PDF]
, 1990 Artemia has a complex extracellular hemoglobin of Mr 260,000 comprising two globin chains (Mr 130,000) each of which is a polymer of eight covalently linked domains of Mr 16,000.
Alard, Philippe +8 more
core +1 more source
Physical and chemical processes and the morphofunctional characteristics of human erythrocytes in hyperglycaemia [PDF]
, 2017 Background: This study examines the effect of graduated hyperglycaemia on the state and oxygen-binding ability of hemoglobin, the correlation of phospholipid fractions and their metabolites in the membrane, the activity of proteolytic enzymes and the ...
Bourdon, Jean Christophe +11 more
core +4 more sources
Thermal-induced proteinquake in oxyhemoglobin [PDF]
arXiv, 2015 Oxygen is released to living tissues via conformational changes of hemoglobin from R-state (oxyhemoglobin) to T-state (desoxyhemoglobin). The detailed mechanism of this process is not yet fully understood. We have carried out micromechanical experiments on oxyhemoglobin crystals to determine the behavior of the Young's modulus and the internal friction
arxiv
Imaging proteins at the truly single-molecule level [PDF]
, 2015 Imaging single proteins has been a long-standing ambition for advancing various fields in natural science, as for instance structural biology, biophysics and molecular nanotechnology. In particular, revealing the distinct conformations of an individual protein is of utmost importance.
arxiv +1 more source
Proceedings of the National Academy of Sciences of the United States of America, 1993 Recent interest in therapies for sickle cell anemia based on elevating fetal Hb has made accurate estimates of the sparing effect of fetal Hb (Hb F) and other non-sickle Hbs on sickle Hb (Hb S) polymerization essential.
W. N. Poillon +4 more
semanticscholar +1 more source
Hubungan Konsumsi Protein Hewani dan Zat Besi dengan Kadar Hemoglobin pada Balita Usia 1336 Bulan [PDF]
, 2006 Children under five years old are the group that susceptible toward the health and nutrition problems. The most prevalence problem is iron deficiency anemia. Most of iron deficiency anemia cases was caused by lack of iron in their meal.
Andarina, D. (Dewi), Sumarmi, S. (Sri)
core
Conformational studies of various hemoglobins by natural-abundance 13C NMR spectroscopy [PDF]
, 1972 Studies of variously liganded hemoglobins (both from human and rabbit) by natural-abundance 13C NMR spectroscopy have revealed apparent conformational differences that have been interpreted on the basis of two quaternary structures for the α2ß2 tetramer,
Moon, R. B., Richards, J. H.
core +1 more source
Association of HMIP1 C-893A polymorphism and disease severity in patients with sickle cell anemia
Hematology, Transfusion and Cell Therapy, 2021 Introduction: Sickle cell anemia (SCA) is a Mendelian disorder with a heterogeneous clinical course. The reasons for this phenotypic diversity are not entirely established, but it is known that high fetal hemoglobin levels lead to a milder course of the ...
Diego A. Pereira-Martins +9 more
doaj