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Anion-pi interactions in active centers of superoxide dismutases

Samo za registrovane korisnike
2018
Autori
Ribić, Vesna
Stojanović, Srđan
Zlatović, Mario
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentu
Apstrakt
We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predic...ted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins.

Ključne reči:
Anion-pi interactions / Superoxide dismutase / Proteins / Active centers / Interaction energy
Izvor:
International Journal of Biological Macromolecules, 2018, 106, 559-568
Izdavač:
  • Elsevier
Finansiranje / projekti:
  • Proučavanje fizičkohemijskih i biohemijskih procesa u životnoj sredini koji utiču na zagađenje i istraživanje mogućnosti za minimiziranje posledica (RS-172001)
  • Interakcije prirodnih proizvoda, njihovih derivata i kompleksnih jedinjenja sa proteinima i nukleinskim kiselinama (RS-172055)
Napomena:
  • The peer-reviewed version: http://cer.ihtm.bg.ac.rs/handle/123456789/3140

DOI: 10.1016/j.ijbiomac.2017.08.050

ISSN: 0141-8130

PubMed: 28811207

WoS: 000417661600063

Scopus: 2-s2.0-85028012582
[ Google Scholar ]
15
9
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/2457
Kolekcije
  • Radovi istraživača / Researchers' publications
Institucija/grupa
IHTM
TY  - JOUR
AU  - Ribić, Vesna
AU  - Stojanović, Srđan
AU  - Zlatović, Mario
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2457
AB  - We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predicted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Anion-pi interactions in active centers of superoxide dismutases
VL  - 106
SP  - 559
EP  - 568
DO  - 10.1016/j.ijbiomac.2017.08.050
ER  - 
@article{
author = "Ribić, Vesna and Stojanović, Srđan and Zlatović, Mario",
year = "2018",
abstract = "We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predicted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Anion-pi interactions in active centers of superoxide dismutases",
volume = "106",
pages = "559-568",
doi = "10.1016/j.ijbiomac.2017.08.050"
}
Ribić, V., Stojanović, S.,& Zlatović, M.. (2018). Anion-pi interactions in active centers of superoxide dismutases. in International Journal of Biological Macromolecules
Elsevier., 106, 559-568.
https://doi.org/10.1016/j.ijbiomac.2017.08.050
Ribić V, Stojanović S, Zlatović M. Anion-pi interactions in active centers of superoxide dismutases. in International Journal of Biological Macromolecules. 2018;106:559-568.
doi:10.1016/j.ijbiomac.2017.08.050 .
Ribić, Vesna, Stojanović, Srđan, Zlatović, Mario, "Anion-pi interactions in active centers of superoxide dismutases" in International Journal of Biological Macromolecules, 106 (2018):559-568,
https://doi.org/10.1016/j.ijbiomac.2017.08.050 . .

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