SARS-CoV-2 protein NSP11
From Proteopedia
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Giri's lab<ref>PMID: 34119626</ref> studied NSP11 in solution and by molecular dynamics. Based on CD, they found that NSP11 shows characteristics of an intrinsically disordered protein (IDP). They further studied the its conformational behavior in the presence of negatively charged and neutral liposomes, and found that it remains disordered. However, in SDS micelle, NSP11 adopts an α-helical conformation, suggesting the helical propensity of NSP11, which is very similar to what [AlphaFold[2 predicts. Based on MD simulations NSP11 appears to to have the behavior of an IDP. | Giri's lab<ref>PMID: 34119626</ref> studied NSP11 in solution and by molecular dynamics. Based on CD, they found that NSP11 shows characteristics of an intrinsically disordered protein (IDP). They further studied the its conformational behavior in the presence of negatively charged and neutral liposomes, and found that it remains disordered. However, in SDS micelle, NSP11 adopts an α-helical conformation, suggesting the helical propensity of NSP11, which is very similar to what [AlphaFold[2 predicts. Based on MD simulations NSP11 appears to to have the behavior of an IDP. | ||
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== See also == | == See also == | ||
Revision as of 15:35, 8 February 2022
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References
- ↑ 1.0 1.1 MIT ColabFold
- ↑ Gadhave K, Kumar P, Kumar A, Bhardwaj T, Garg N, Giri R. Conformational dynamics of 13 amino acids long NSP11 of SARS-CoV-2 under membrane mimetics and different solvent conditions. Microb Pathog. 2021 Sep;158:105041. doi: 10.1016/j.micpath.2021.105041. Epub 2021, Jun 10. PMID:34119626 doi:http://dx.doi.org/10.1016/j.micpath.2021.105041
