| Autor: |
Enciso, Marta, Schuette, Christof, Site, Luigi Delle |
| Rok vydání: |
2013 |
| Předmět: |
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| Druh dokumentu: |
Working Paper |
| DOI: |
10.1080/00268976.2013.827254 |
| Popis: |
In a recent work we proposed a coarse-grained methodology for studying the response of peptides when simulated at different values of pH; in this work we extend the methodology to analyze the pH-dependent behavior of coiled coils. This protein structure presents a remarkable chain stiffness andis formed by two or more long helical peptides that are interacting like the strands of a rope. Chain length and rigidity are the key aspects needed to extend previous peptide interaction potentials to this particular case; however the original model is naturally recovered when the length or the ridigity of the simulated chain are reduced. We apply the model and discuss results for two cases: (a) the folding/unfolding transition of a generic coiled coil as a function of pH; (b) behavior of a specific sequence as a function of the acidity conditions. In this latter case results are compared with experimental data from the literature in order to comment about the consistency of our approach. |
| Databáze: |
arXiv |
| Externí odkaz: |
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