Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins

[Image: see text] We present a new coarse-grained C(α)-based protein model with a nonradial multibody pseudo-improper-dihedral potential that is transferable, time-independent, and suitable for molecular dynamics. It captures the nature of backbone and side-chain interactions between amino acid resi...

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Autores principales: Mioduszewski, Łukasz, Różycki, Bartosz, Cieplak, Marek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7588027/
https://www.ncbi.nlm.nih.gov/pubmed/32436706
http://dx.doi.org/10.1021/acs.jctc.0c00338
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author Mioduszewski, Łukasz
Różycki, Bartosz
Cieplak, Marek
author_facet Mioduszewski, Łukasz
Różycki, Bartosz
Cieplak, Marek
author_sort Mioduszewski, Łukasz
collection PubMed
description [Image: see text] We present a new coarse-grained C(α)-based protein model with a nonradial multibody pseudo-improper-dihedral potential that is transferable, time-independent, and suitable for molecular dynamics. It captures the nature of backbone and side-chain interactions between amino acid residues by adapting a simple improper dihedral term for a one-bead-per-residue model. It is parameterized for intrinsically disordered proteins and applicable to simulations of such proteins and their assemblies on millisecond time scales.
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spelling pubmed-75880272020-10-27 Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins Mioduszewski, Łukasz Różycki, Bartosz Cieplak, Marek J Chem Theory Comput [Image: see text] We present a new coarse-grained C(α)-based protein model with a nonradial multibody pseudo-improper-dihedral potential that is transferable, time-independent, and suitable for molecular dynamics. It captures the nature of backbone and side-chain interactions between amino acid residues by adapting a simple improper dihedral term for a one-bead-per-residue model. It is parameterized for intrinsically disordered proteins and applicable to simulations of such proteins and their assemblies on millisecond time scales. American Chemical Society 2020-05-21 2020-07-14 /pmc/articles/PMC7588027/ /pubmed/32436706 http://dx.doi.org/10.1021/acs.jctc.0c00338 Text en This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
spellingShingle Mioduszewski, Łukasz
Różycki, Bartosz
Cieplak, Marek
Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins
title Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins
title_full Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins
title_fullStr Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins
title_full_unstemmed Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins
title_short Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins
title_sort pseudo-improper-dihedral model for intrinsically disordered proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7588027/
https://www.ncbi.nlm.nih.gov/pubmed/32436706
http://dx.doi.org/10.1021/acs.jctc.0c00338
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AT cieplakmarek pseudoimproperdihedralmodelforintrinsicallydisorderedproteins

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