Article ; Online: Structural stability of R-state conformation of carbonmonoxyl sickle and normal hemoglobin dimer.
Journal of biomolecular structure & dynamics
2022 Volume 41, Issue 19, Page(s) 9957–9966
Abstract: A mutation at the sixth residue, glutamic acid to valine, in beta chain of hemoglobin distorts the entire shape of hemoglobin into a sickle shape. The investigation of the binding mechanisms of different chains of hemoglobin under the mutated condition ... ...
| Abstract | A mutation at the sixth residue, glutamic acid to valine, in beta chain of hemoglobin distorts the entire shape of hemoglobin into a sickle shape. The investigation of the binding mechanisms of different chains of hemoglobin under the mutated condition can give an understanding of the molecular distortion. In this work, we have studied the binding mechanism between two chains in the dimer structure of the R-state conformation of carbonmonoxyl sickle hemoglobin and is compared with that of normal hemoglobin by using molecular dynamics simulations. The binding strength between |
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| MeSH term(s) | Humans ; Hemoglobins/chemistry ; Protein Conformation ; Molecular Dynamics Simulation ; Hemoglobin, Sickle ; Anemia, Sickle Cell/metabolism | |||||
| Chemical Substances | Hemoglobins ; Hemoglobin, Sickle | |||||
| Language | English | |||||
| Publishing date | 2022-12-06 | |||||
| Publishing country | England | |||||
| Document type | Journal Article ; Research Support, Non-U.S. Gov't | |||||
| ZDB-ID | 49157-3 | |||||
| ISSN | 1538-0254 ; 0739-1102 | |||||
| ISSN (online) | 1538-0254 | |||||
| ISSN | 0739-1102 | |||||
| DOI | 10.1080/07391102.2022.2150890 | |||||
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| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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