Synthetic polymers as substrates for a DNA‐sliding clamp protein

The clamp protein (gp45) of the DNA polymerase III of the bacteriophage T4 is known to bind to DNA and stay attached to it in order to facilitate the process of DNA copying by the polymerase. As part of a project aimed at developing new biomimetic data‐encoding systems we have investigated the bindi...

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Detalles Bibliográficos
Autores principales: van Dongen, S. F. M., Clerx, J., van den Boomen, O. I., Pervaiz, M., Trakselis, M. A., Ritschel, T., Schoonen, L., Schoenmakers, D. C., Nolte, R. J. M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Original Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6001473/
https://www.ncbi.nlm.nih.gov/pubmed/29700825
http://dx.doi.org/10.1002/bip.23119
Descripción
Sumario:The clamp protein (gp45) of the DNA polymerase III of the bacteriophage T4 is known to bind to DNA and stay attached to it in order to facilitate the process of DNA copying by the polymerase. As part of a project aimed at developing new biomimetic data‐encoding systems we have investigated the binding of gp45 to synthetic polymers, that is, rigid, helical polyisocyanopeptides. Molecular modelling studies suggest that the clamp protein may interact with the latter polymers. Experiments aimed at verifying these interactions are presented and discussed.

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