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Modulation of folding energy landscape by charge–charge interactions: Linking experiments with computational modeling
The kinetics of folding–unfolding of a structurally diverse set of four proteins optimized for thermodynamic stability by rational redesign of surface charge–charge interactions is characterized experimentally. The folding rates are faster for designed variants compared with their wild-type proteins...
Tallennettuna:
| Julkaisussa: | Proc Natl Acad Sci U S A |
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| Päätekijät: | , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
2015
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4311858/ https://ncbi.nlm.nih.gov/pubmed/25564663 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1410424112 |
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