TY  - DATA
AU  - Jovanović, Milena
AU  - Gruden-Pavlović, Maja
AU  - Zlatović, Mario
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3423
PB  - Springer Wien, Wien
T2  - Monatshefte Fur Chemie
T1  - Supplementary data for article: Jovanović, M.; Gruden-Pavlović, M.; Zlatović, M. Stabilizing Non-Covalent Interactions of Ligand Aromatic Moieties and Proline in Ligand-Protein Systems. Monatshefte fur Chemie 2015, 146 (2), 389–397. https://doi.org/10.1007/s00706-014-1357-8
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3423
ER  - 

@misc{
author = "Jovanović, Milena and Gruden-Pavlović, Maja and Zlatović, Mario",
year = "2015",
publisher = "Springer Wien, Wien",
journal = "Monatshefte Fur Chemie",
title = "Supplementary data for article: Jovanović, M.; Gruden-Pavlović, M.; Zlatović, M. Stabilizing Non-Covalent Interactions of Ligand Aromatic Moieties and Proline in Ligand-Protein Systems. Monatshefte fur Chemie 2015, 146 (2), 389–397. https://doi.org/10.1007/s00706-014-1357-8",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3423"
}

Jovanović, M., Gruden-Pavlović, M.,& Zlatović, M.. (2015). Supplementary data for article: Jovanović, M.; Gruden-Pavlović, M.; Zlatović, M. Stabilizing Non-Covalent Interactions of Ligand Aromatic Moieties and Proline in Ligand-Protein Systems. Monatshefte fur Chemie 2015, 146 (2), 389–397. https://doi.org/10.1007/s00706-014-1357-8. in Monatshefte Fur Chemie
Springer Wien, Wien..
https://hdl.handle.net/21.15107/rcub_cherry_3423

Jovanović M, Gruden-Pavlović M, Zlatović M. Supplementary data for article: Jovanović, M.; Gruden-Pavlović, M.; Zlatović, M. Stabilizing Non-Covalent Interactions of Ligand Aromatic Moieties and Proline in Ligand-Protein Systems. Monatshefte fur Chemie 2015, 146 (2), 389–397. https://doi.org/10.1007/s00706-014-1357-8. in Monatshefte Fur Chemie. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3423 .

Jovanović, Milena, Gruden-Pavlović, Maja, Zlatović, Mario, "Supplementary data for article: Jovanović, M.; Gruden-Pavlović, M.; Zlatović, M. Stabilizing Non-Covalent Interactions of Ligand Aromatic Moieties and Proline in Ligand-Protein Systems. Monatshefte fur Chemie 2015, 146 (2), 389–397. https://doi.org/10.1007/s00706-014-1357-8" in Monatshefte Fur Chemie (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3423 .

TY  - JOUR
AU  - Jovanović, Milena
AU  - Gruden-Pavlović, Maja
AU  - Zlatović, Mario
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1652
AB  - Proline, due to its conformational specificity, is known to show some unique properties and has significant functions in the tertiary structure of proteins. It was suggested that proline could have an important influence on some vital interactions in protein as well, by engaging in non-covalent stabilization interactions with some aromatic moieties. In this work, the interactions that occur between proline and some aromatic moieties in ligands were investigated by means of the density functional theory using an exchange-correlation functional capable of taking into account dispersion interactions. The obtained results showed that the stabilization energy between a properly placed proline and an aromatic moiety could be as large as 25 kJ/mol and hence be a significant factor in placing a ligand in binding site of a protein. This indicates that the error in determining the most favorable structure of ligand-protein complexes obtained by usual molecular docking experiments sometimes could be the result of neglecting this type of interactions.
PB  - Springer Wien, Wien
T2  - Monatshefte Fur Chemie
T1  - Stabilizing non-covalent interactions of ligand aromatic moieties and proline in ligand-protein systems
VL  - 146
IS  - 2
SP  - 389
EP  - 397
DO  - 10.1007/s00706-014-1357-8
ER  - 

@article{
author = "Jovanović, Milena and Gruden-Pavlović, Maja and Zlatović, Mario",
year = "2015",
abstract = "Proline, due to its conformational specificity, is known to show some unique properties and has significant functions in the tertiary structure of proteins. It was suggested that proline could have an important influence on some vital interactions in protein as well, by engaging in non-covalent stabilization interactions with some aromatic moieties. In this work, the interactions that occur between proline and some aromatic moieties in ligands were investigated by means of the density functional theory using an exchange-correlation functional capable of taking into account dispersion interactions. The obtained results showed that the stabilization energy between a properly placed proline and an aromatic moiety could be as large as 25 kJ/mol and hence be a significant factor in placing a ligand in binding site of a protein. This indicates that the error in determining the most favorable structure of ligand-protein complexes obtained by usual molecular docking experiments sometimes could be the result of neglecting this type of interactions.",
publisher = "Springer Wien, Wien",
journal = "Monatshefte Fur Chemie",
title = "Stabilizing non-covalent interactions of ligand aromatic moieties and proline in ligand-protein systems",
volume = "146",
number = "2",
pages = "389-397",
doi = "10.1007/s00706-014-1357-8"
}

Jovanović, M., Gruden-Pavlović, M.,& Zlatović, M.. (2015). Stabilizing non-covalent interactions of ligand aromatic moieties and proline in ligand-protein systems. in Monatshefte Fur Chemie
Springer Wien, Wien., 146(2), 389-397.
https://doi.org/10.1007/s00706-014-1357-8

Jovanović M, Gruden-Pavlović M, Zlatović M. Stabilizing non-covalent interactions of ligand aromatic moieties and proline in ligand-protein systems. in Monatshefte Fur Chemie. 2015;146(2):389-397.
doi:10.1007/s00706-014-1357-8 .

Jovanović, Milena, Gruden-Pavlović, Maja, Zlatović, Mario, "Stabilizing non-covalent interactions of ligand aromatic moieties and proline in ligand-protein systems" in Monatshefte Fur Chemie, 146, no. 2 (2015):389-397,
https://doi.org/10.1007/s00706-014-1357-8 . .