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10.1080/07391102.2021.1872418

http://scihub22266oqcxt.onion/10.1080/07391102.2021.1872418
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suck abstract from ncbi


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pmid33475020      J+Biomol+Struct+Dyn 2022 ; 40 (12): 5634-5642
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  • Insight into molecular characteristics of SARS-CoV-2 spike protein following D614G point mutation, a molecular dynamics study #MMPMID33475020
  • Mahmoudi Gomari M; Rostami N; Omidi-Ardali H; Arab SS
  • J Biomol Struct Dyn 2022[Aug]; 40 (12): 5634-5642 PMID33475020show ga
  • Undoubtedly, the SARS-CoV-2 has become a major concern for all societies due to its catastrophic effects on public health. In addition, mutations and changes in the structure of the virus make it difficult to design effective treatment. Moreover, the amino acid sequence of a protein is a major factor in the formation of the second and tertiary structure in a protein. Amino acid replacement can have noticeable effects on the folding of a protein, especially if an asymmetric change (substitution of polar residue with non-polar, charged with an uncharged, positive charge with a negative charge, or large residue with small residue) occurs. D614G as a spike mutant of SARS-CoV-2 previously identified as an associated risk factor with a high mortality rate of this virus. Using structural bioinformatics, our group determined that D614G mutation could cause extensive changes in SARS-CoV-2 behavior including the secondary structure, receptor binding pattern, 3D conformation, and stability of it.Communicated by Ramaswamy H. Sarma.
  • |*COVID-19/genetics[MESH]
  • |*Spike Glycoprotein, Coronavirus/chemistry/genetics/metabolism[MESH]
  • |Humans[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Mutation[MESH]
  • |Point Mutation[MESH]


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