Structural heterogeneity and precision of implications drawn from cryo-electron microscopy structures: SARS-CoV-2 spike-protein mutations as a test case
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
https://link.springer.com/content/pdf/10.1007/s00249-022-01619-8.pdf
Reference85 articles.
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2. Bæk KT, Kepp KP (2022a) Data set and fitting dependencies when estimating protein mutant stability: toward simple, balanced, and interpretable models. J Comput Chem 43:504–518. https://doi.org/10.1002/jcc.26810
3. Bæk KT, Kepp KP (2022b) Assessment of AlphaFold2 for human proteins via residue solvent exposure. J Chem Inf Model 62:3391–3400. https://doi.org/10.1021/acs.jcim.2c00243
4. Berger I, Schaffitzel C (2020) The SARS-CoV-2 spike protein: balancing stability and infectivity. Cell Res 30:1059–1060. https://doi.org/10.1038/s41422-020-00430-4
5. Bershtein S, Goldin K, Tawfik DS (2008) Intense neutral drifts yield robust and evolvable consensus proteins. J Mol Biol 379:1029–1044. https://doi.org/10.1016/j.jmb.2008.04.024
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