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Quantitative Analysis of Protein Unfolded State Energetics: Experimental and Computational Studies Demonstrate That Non-Native Side-Chain Interactions Stabilize Local Native Backbone Structure.
Proteins fold on relatively smooth free energy landscapes which are biased towards the native state, but even simple topologies which fold rapidly, can experience roughness on their free energy landscape. The details of these interactions are difficult to elucidate experimentally. Closely related to...
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| Publicat a: | J Phys Chem B |
|---|---|
| Autors principals: | , , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
2021
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC8197028/ https://ncbi.nlm.nih.gov/pubmed/33779182 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.jpcb.0c08922 |
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