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Side chain flexibility and the symmetry of protein homodimers
A comprehensive analysis of crystallographic data of 565 high-resolution protein homodimers comprised of over 250,000 residues suggests that amino acids form two groups that differ in their tendency to distort or symmetrize the structure of protein homodimers. Residues of the first group tend to dis...
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| Vydáno v: | PLoS One |
|---|---|
| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Public Library of Science
2020
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7380632/ https://ncbi.nlm.nih.gov/pubmed/32706779 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0235863 |
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