Protein structure analysis of abnormal hemoglobins; Hb D-Los Angeles, Hb S and Hb G-Coushatta
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Tarih
2024
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info:eu-repo/semantics/openAccess
Özet
Computational methods have been extensively utilized for protein structure prediction and modeling, including hemoglobin. These methods have provided valuable insights into the three-dimensional conformation of hemoglobin, its allosteric regulation, and its oxygen-binding capacity. For instance, computational modeling has been employed to understand the structural mechanism of hemoglobin, shedding light on the equilibrium between alternative structures, like the tense (T) and relaxed (R) states, which influence oxygen affinity and binding. Abnormal hemoglobins are associated with various genetic and clinical implications. The mutations in the globin genes to cause changes in the molecular structure of hemoglobin, affecting its biological properties such as oxygen carrying capacity and stability. RMSD is the mean displacement of atoms or molecular structures. Therefore, RMSD is a preferred parameter in structural similarity modeling studies. RMSD values calculated for pairwise protein structures are Hb A (Normal Hb)-Hb D-Los Angeles 3.44 Å, Hb A-Hb S 3.339 Å, Hb A-Hb G-Coushatta 3.35 Å. The aim of this study is to discuss the possible structural and electrical properties of abnormal haemoglobin molecules using protein modelling.
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#DEĞER!
Kaynak
Medicine Science
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Cilt
13
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2
