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Convergence of atomic charges with the size of the enzymatic environment

Danny Vanpoucke, J Olah, F De Proft, Veronique Van Speybroeck UGent and G Roos (2015) JOURNAL OF CHEMICAL INFORMATION AND MODELING. 55(3). p.564-571
abstract
Atomic charges are a key concept to give more insight into the electronic structure and chemical reactivity. The Hirshfeld-I partitioning scheme applied to the model protein human 2-cysteine peroxiredoxin thioredoxin peroxidase B is used to investigate how large a protein fragment needs to be in order to achieve convergence of the atomic charge of both neutral and negatively charged residues. Convergence in atomic charges is rapidly reached for neutral residues, but not for negatively charged ones. This study pinpoints difficulties on the road toward accurate modeling of negatively charged residues of large biomolecular systems in a multiscale approach.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
EXTENDING HIRSHFELD-I, DENSITY-FUNCTIONAL THEORY, DYNAMICS SIMULATIONS, PERIODIC MATERIALS, ORGANIC-MOLECULES, PK(A) VALUES, FORCE-FIELD, PROTEINS, MOLECULAR WAVE FUNCTIONS, ELECTRONIC POPULATION ANALYSIS
journal title
JOURNAL OF CHEMICAL INFORMATION AND MODELING
J. Chem Inf. Model.
volume
55
issue
3
pages
564 - 571
Web of Science type
Article
Web of Science id
000351652900009
JCR category
COMPUTER SCIENCE, INFORMATION SYSTEMS
JCR impact factor
3.657 (2015)
JCR rank
6/143 (2015)
JCR quartile
1 (2015)
ISSN
1549-9596
DOI
10.1021/ci5006417
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
5944634
handle
http://hdl.handle.net/1854/LU-5944634
date created
2015-04-28 08:47:55
date last changed
2016-12-19 15:40:03
@article{5944634,
  abstract     = {Atomic charges are a key concept to give more insight into the electronic structure and chemical reactivity. The Hirshfeld-I partitioning scheme applied to the model protein human 2-cysteine peroxiredoxin thioredoxin peroxidase B is used to investigate how large a protein fragment needs to be in order to achieve convergence of the atomic charge of both neutral and negatively charged residues. Convergence in atomic charges is rapidly reached for neutral residues, but not for negatively charged ones. This study pinpoints difficulties on the road toward accurate modeling of negatively charged residues of large biomolecular systems in a multiscale approach.},
  author       = {Vanpoucke, Danny and Olah, J and De Proft, F and Van Speybroeck, Veronique and Roos, G},
  issn         = {1549-9596},
  journal      = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
  keyword      = {EXTENDING HIRSHFELD-I,DENSITY-FUNCTIONAL THEORY,DYNAMICS SIMULATIONS,PERIODIC MATERIALS,ORGANIC-MOLECULES,PK(A) VALUES,FORCE-FIELD,PROTEINS,MOLECULAR WAVE FUNCTIONS,ELECTRONIC POPULATION ANALYSIS},
  language     = {eng},
  number       = {3},
  pages        = {564--571},
  title        = {Convergence of atomic charges with the size of the enzymatic environment},
  url          = {http://dx.doi.org/10.1021/ci5006417},
  volume       = {55},
  year         = {2015},
}

Chicago
Vanpoucke, Danny, J Olah, F De Proft, Veronique Van Speybroeck, and G Roos. 2015. “Convergence of Atomic Charges with the Size of the Enzymatic Environment.” Journal of Chemical Information and Modeling 55 (3): 564–571.
APA
Vanpoucke, Danny, Olah, J., De Proft, F., Van Speybroeck, V., & Roos, G. (2015). Convergence of atomic charges with the size of the enzymatic environment. JOURNAL OF CHEMICAL INFORMATION AND MODELING, 55(3), 564–571.
Vancouver
1.
Vanpoucke D, Olah J, De Proft F, Van Speybroeck V, Roos G. Convergence of atomic charges with the size of the enzymatic environment. JOURNAL OF CHEMICAL INFORMATION AND MODELING. 2015;55(3):564–71.
MLA
Vanpoucke, Danny, J Olah, F De Proft, et al. “Convergence of Atomic Charges with the Size of the Enzymatic Environment.” JOURNAL OF CHEMICAL INFORMATION AND MODELING 55.3 (2015): 564–571. Print.