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10.1002/pro.4097

http://scihub22266oqcxt.onion/10.1002/pro.4097
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33934422!8242659!33934422
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suck abstract from ncbi


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pmid33934422      Protein+Sci 2021 ; 30 (8): 1723-1729
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  • Predictable fold switching by the SARS-CoV-2 protein ORF9b #MMPMID33934422
  • Porter LL
  • Protein Sci 2021[Aug]; 30 (8): 1723-1729 PMID33934422show ga
  • Extant fold-switching proteins remodel their secondary structures and change their functions in response to environmental stimuli. These shapeshifting proteins regulate biological processes and are associated with a number of diseases, including tuberculosis, cancer, Alzheimer's, and autoimmune disorders. Thus, predictive methods are needed to identify more fold-switching proteins, especially since all naturally occurring instances have been discovered by chance. In response to this need, two high-throughput predictive methods have recently been developed. Here we test them on ORF9b, a newly discovered fold switcher and potential therapeutic target from the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2). Promisingly, both methods correctly indicate that ORF9b switches folds. We then tested the same two methods on ORF9b1, the ORF9b homolog from SARS-CoV-1. Again, both methods predict that ORF9b1 switches folds, a finding consistent with experimental binding studies. Together, these results (a) demonstrate that protein fold switching can be predicted using high-throughput computational approaches and (b) suggest that fold switching might be a general characteristic of ORF9b homologs.
  • |Coronavirus Nucleocapsid Proteins/*chemistry/genetics/metabolism[MESH]
  • |Humans[MESH]
  • |Models, Molecular[MESH]
  • |Phosphoproteins/chemistry/genetics/metabolism[MESH]
  • |Protein Folding[MESH]
  • |Protein Structure, Secondary[MESH]


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