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...

Descripción completa

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
_version_ 1783332012176703488
author 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.
author_facet 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.
author_sort van Dongen, S. F. M.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-6001473
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher John Wiley and Sons Inc.
record_format MEDLINE/PubMed
spelling pubmed-60014732018-06-21 Synthetic polymers as substrates for a DNA‐sliding clamp protein 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. Biopolymers Original Articles 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. John Wiley and Sons Inc. 2018-04-26 2018-05 /pmc/articles/PMC6001473/ /pubmed/29700825 http://dx.doi.org/10.1002/bip.23119 Text en © 2018 The Authors Biopolymers Published by Wiley Periodicals, Inc. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Original Articles
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.
Synthetic polymers as substrates for a DNA‐sliding clamp protein
title Synthetic polymers as substrates for a DNA‐sliding clamp protein
title_full Synthetic polymers as substrates for a DNA‐sliding clamp protein
title_fullStr Synthetic polymers as substrates for a DNA‐sliding clamp protein
title_full_unstemmed Synthetic polymers as substrates for a DNA‐sliding clamp protein
title_short Synthetic polymers as substrates for a DNA‐sliding clamp protein
title_sort synthetic polymers as substrates for a dna‐sliding clamp protein
topic Original Articles
url 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
work_keys_str_mv AT vandongensfm syntheticpolymersassubstratesforadnaslidingclampprotein
AT clerxj syntheticpolymersassubstratesforadnaslidingclampprotein
AT vandenboomenoi syntheticpolymersassubstratesforadnaslidingclampprotein
AT pervaizm syntheticpolymersassubstratesforadnaslidingclampprotein
AT trakselisma syntheticpolymersassubstratesforadnaslidingclampprotein
AT ritschelt syntheticpolymersassubstratesforadnaslidingclampprotein
AT schoonenl syntheticpolymersassubstratesforadnaslidingclampprotein
AT schoenmakersdc syntheticpolymersassubstratesforadnaslidingclampprotein
AT nolterjm syntheticpolymersassubstratesforadnaslidingclampprotein

Ejemplares similares