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DNA polymerase conformational dynamics and the role of fidelity-conferring residues: Insights from computational simulations

Abstract:

Herein we investigate the molecular bases of DNA polymerase I conformational dynamics that underlie the replication fidelity of the enzyme. Such fidelity is determined by conformational changes that promote the rejection of incorrect nucleotides before the chemical ligation step. We report a comprehensive atomic resolution study of wild type and mutant enzymes in different bound states and starting from different crystal structures, using extensive molecular dynamics (MD) simulations that cov...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.3389/fmolb.2016.00020

Authors


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Role:
Author
ORCID:
0000-0003-3304-6104
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Role:
Author
ORCID:
0000-0002-7121-0609
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Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Sub department:
Condensed Matter Physics
Oxford college:
St Cross College
Role:
Author
ORCID:
0000-0002-0904-5323
Publisher:
Frontiers Media Publisher's website
Journal:
Frontiers in Molecular Biosciences Journal website
Volume:
3
Issue:
MAY
Article number:
20
Publication date:
2016-05-27
Acceptance date:
2016-05-10
DOI:
EISSN:
2296-889X
Pmid:
27303671
Source identifiers:
628301
Language:
English
Keywords:
Pubs id:
pubs:628301
UUID:
uuid:3fb6a57f-fb1e-41a0-9c2b-4facc621c9df
Local pid:
pubs:628301
Deposit date:
2019-02-07

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