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Updated: Jul 17, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Analysis of functional aberration of some important beta hemoglobinopathies (hemoglobin C, D, E, and S) from
1Department of Laboratory Medicine, Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand. wviroj@pioneer.netserv.chula.ac.th <wviroj@pioneer.netserv.chula.ac.th>
Hemoglobinopathy comprises a group of inherited hemoglobin disorders in which hemoglobin (Hb) was improperly formed, but the cause is not depletion of the globin gene. Typically, when the basic pathogenesis is a single substitution disorder, only one aberration presents in the secondary structure. However, the manifested or functional aberration resulting from the structural aberration usually varies. It is sometimes difficult to compare the degree of functional aberration among such hemoglobin disorders. A functional analysis was performed on 4 important beta hemoglobinopathies (hemoglobin C, D, E, and S) using PolyPhen, a novel bioinformatic tool. The mutations Hb C (beta 6, Glu --> Lys), Hb D (beta 121, Glu --> Gln), Hb E (beta 26, Glu --> Lys), and Hb S (beta 6, Glu --> Val) were selected for further study. According to the in silico mutation study, the functional change in the studied hemoglobinopathies was variable. The position-specific independent counts (PSIC) difference score ranged from 1.362 (Hb D) to 2.986 (Hb S). Regarding the degree of damage, all had probable damage. This analysis demonstrated that the functional aberration in the hemoglobinopathy was based on complex pathogenesis. Identifying only the structural aberration in a hemoglobinopathy is not sufficient; additional functional analysis is recommended. The functional analysis presented here may be a good model for further research.
Hemoglobinopathy comprises a group of inherited hemoglobin disorders in which hemoglobin (Hb) was improperly formed, but the cause is not depletion of the globin gene. Typically, when the basic pathogenesis is a single substitution disorder, only one aberration presents in the secondary structure. However, the manifested or functional aberration resulting from the structural aberration usually varies. It is sometimes difficult to compare the degree of functional aberration among such hemoglobin disorders. A functional analysis was performed on 4 important beta hemoglobinopathies (hemoglobin C, D, E, and S) using PolyPhen, a novel bioinformatic tool. The mutations Hb C (beta 6, Glu --> Lys), Hb D (beta 121, Glu --> Gln), Hb E (beta 26, Glu --> Lys), and Hb S (beta 6, Glu --> Val) were selected for further study. According to the in silico mutation study, the functional change in the studied hemoglobinopathies was variable. The position-specific independent counts (PSIC) difference score ranged from 1.362 (Hb D) to 2.986 (Hb S). Regarding the degree of damage, all had probable damage. This analysis demonstrated that the functional aberration in the hemoglobinopathy was based on complex pathogenesis. Identifying only the structural aberration in a hemoglobinopathy is not sufficient; additional functional analysis is recommended. The functional analysis presented here may be a good model for further research.
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