| Autor: |
X. Viader-Godoy, C. R. Pulido, B. Ibarra, M. Manosas, F. Ritort |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| Zdroj: |
Physical Review X, Vol 11, Iss 3, p 031037 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2160-3308 |
| DOI: |
10.1103/PhysRevX.11.031037 |
| Popis: |
The folding of biological macromolecules is a fundamental process of which we lack a full comprehension. Mostly studied in proteins and RNA, single-stranded DNA (ssDNA) also folds, at physiological salt conditions, by forming nonspecific secondary structures that are difficult to characterize with biophysical techniques. Here, we present a helix-coil model for secondary-structure formation, where ssDNA bases are organized in two different types of domains (compact and free). The model contains two parameters: the energy gain per base in a compact domain, ε, and the cooperativity related to the interfacial energy between different domains, γ. We test the ability of the model to quantify the formation of secondary structure in ssDNA molecules mechanically stretched with optical tweezers. The model reproduces the experimental force-extension curves in ssDNA of different molecular lengths and varying sodium and magnesium concentrations. Salt-correction effects for the energy of compact domains and the interfacial energy are found to be compatible with those of DNA hybridization. The model also predicts the folding free energy and the average size of domains at zero force, finding good agreement with secondary-structure predictions by mfold. We envision the model could be further extended to investigate native folding in RNA and proteins. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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